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Conserved domains on  [gi|695706061|ref|WP_032641296|]
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MULTISPECIES: murein DD-endopeptidase MepM [Enterobacter cloacae complex]

Protein Classification

murein DD-endopeptidase MepM( domain architecture ID 11485447)

murein DD-endopeptidase MepM is thought to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11649 PRK11649
putative peptidase; Provisional
 1-439 0e+00

putative peptidase; Provisional


:

Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 980.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061   1 MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPSSAPIIKTIELEKSEIRSLLPEASEPIDQAAQEDEAI 80
Cdd:PRK11649   1 MQQIARSIALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPESAPIVKTIELEKSEIRSLLPEASEPIDQAAQEDEAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  81 PQDELDDKTENEAGIHEYVVSTGDTLSSVLNQYGIDMGNISQLAAADKDLRNLKIGQQLSWTLTADGDLQRLTWEMSRRE 160
Cdd:PRK11649  81 PQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMSDISQLAAQDKELRNLKIGQQLSWTLTADGDLQRLTWEVSRRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 161 TRTYDRTANGFKMTSEMQKGDWVNNVLKGTVGASFVSSARDAGLTSGEISSVIKAMQWQMDFRKLKKGDEFSVLMSREML 240
Cdd:PRK11649 161 TRTYDRTGNGFKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEISAVIKALQWQMDFRKLKKGDEFSVLMSREML 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 241 DGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKQFRVSSNFNPRRLNPVTGRVAPHRGVDFAM 320
Cdd:PRK11649 241 DGKSEQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRFPTAKQFRISSNFNPRRLNPVTGRVAPHRGVDFAM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 321 PQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGPHLHYEVWIN 400
Cdd:PRK11649 321 PVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWIN 400

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 695706061 401 QQAVNPLTAKLPRTEGLTGKDRTDYLAQVKEVIPQLSLN 439
Cdd:PRK11649 401 QQAVNPLTAKLPRTEGLTGKDRREYLAQVKEVVPQLRFD 439
 
Name Accession Description Interval E-value
PRK11649 PRK11649
putative peptidase; Provisional
 1-439 0e+00

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 980.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061   1 MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPSSAPIIKTIELEKSEIRSLLPEASEPIDQAAQEDEAI 80
Cdd:PRK11649   1 MQQIARSIALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPESAPIVKTIELEKSEIRSLLPEASEPIDQAAQEDEAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  81 PQDELDDKTENEAGIHEYVVSTGDTLSSVLNQYGIDMGNISQLAAADKDLRNLKIGQQLSWTLTADGDLQRLTWEMSRRE 160
Cdd:PRK11649  81 PQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMSDISQLAAQDKELRNLKIGQQLSWTLTADGDLQRLTWEVSRRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 161 TRTYDRTANGFKMTSEMQKGDWVNNVLKGTVGASFVSSARDAGLTSGEISSVIKAMQWQMDFRKLKKGDEFSVLMSREML 240
Cdd:PRK11649 161 TRTYDRTGNGFKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEISAVIKALQWQMDFRKLKKGDEFSVLMSREML 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 241 DGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKQFRVSSNFNPRRLNPVTGRVAPHRGVDFAM 320
Cdd:PRK11649 241 DGKSEQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRFPTAKQFRISSNFNPRRLNPVTGRVAPHRGVDFAM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 321 PQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGPHLHYEVWIN 400
Cdd:PRK11649 321 PVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWIN 400

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 695706061 401 QQAVNPLTAKLPRTEGLTGKDRTDYLAQVKEVIPQLSLN 439
Cdd:PRK11649 401 QQAVNPLTAKLPRTEGLTGKDRREYLAQVKEVVPQLRFD 439
Csd3_N2 pfam19425
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This ...
 179-300 4.11e-86

Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This domain has a similar structure to pfam18059 despite low sequence similarity.


Pssm-ID: 437257 [Multi-domain]  Cd Length: 122  Bit Score: 258.49  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  179 KGDWVNNVLKGTVGASFVSSARDAGLTSGEISSVIKAMQWQMDFRKLKKGDEFSVLMSREMLDGKREQSQLLGVRLRSEG 258
Cdd:pfam19425   1 EGEWQNSVLKGRVDGSFVASARKAGLTSNEISAVIKALQWQLDFRKLKKGDKFSVLMSREMLDGKREQSQLLGVRLRSGG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 695706061  259 KDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKQFRVSSNFNP 300
Cdd:pfam19425  81 KDYYAIRAEDGKFYDRNGSGLARGFLRFPTAKQFRVSSNFNP 122
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 12-422 7.32e-63

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 209.14  E-value: 7.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  12 FNNLPRPHRVMLGSLTVLTLaVAVWRPYVYHPSSAPIIKTIELEkSEIRSLLPEASEPIDQAAQEDEAipqdelddkten 91
Cdd:COG3061    4 MNPLPRKHRRLLGLLSALLL-LALLLPSPDASASRVSQPLVPLA-LTAEADAPAAAAPAAPAAPEGEW------------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  92 eagiHEYVVSTGDTLSSVLNQYGIDMGNISQLAAAD---KDLRNLKIGQQLSWTLTADGDLQRLTWEMSRRETRTYDRTA 168
Cdd:COG3061   70 ----QEYTVQSGDTLSQIFRRLGLSASDLYALLAAEgdaKPLSRLKPGQELRFQLDADGQLQALRYEVSRLETLLFTRQG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 169 NGFKMTSEMqkgdwvnnvlkGTVGASFVSSARDAGLTSGEISSVIKAMQWQMDFRKLKKGDEFSVLMSREMLDGKREQSQ 248
Cdd:COG3061  146 DGFQRKRVT-----------ELSDGSFSADAALASLETLELAAAAGILSDFIAAALDAGAGDAGLVELEIILDDDIDFAD 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 249 LLGVRLRSEGKDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKQFRVSSNFNPRRLNP----------------------- 305
Cdd:COG3061  215 LLFAADRFTGDYFRVYAEGEGGDGGYIGAGGFRAAKFRRRAVRFRRSSSSSSYRRRPhrlsrrrrlrrgpdaaapsgssn 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 306 --------VTGRVAPHRGVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGD 377
Cdd:COG3061  295 aagggghkITRRGGGGGGAAVGVGTGTPTTGAGLGVVRGGRGGGGGVVVGQIGRGGTYGGTGLHLHKHGHKGGGVVGQGV 374

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 695706061 378 RIAISGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDR 422
Cdd:COG3061  375 TIGTLGGTGPTTGPHLHYEFVQNGVRVAPLTVKLPAAPPLAAAAA 419
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 313-397 1.59e-42

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 144.66  E-value: 1.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 313 HRGVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGPH 392
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                 ....*
gi 695706061 393 LHYEV 397
Cdd:cd12797   81 LHFEI 85
LysM smart00257
Lysin motif;
97-141 1.21e-05

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 42.05  E-value: 1.21e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 695706061    97 EYVVSTGDTLSSVLNQYGIDMgniSQLAAADKDL--RNLKIGQQLSW 141
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISV---SDLLELNNILdpDNLQVGQKLKI 44
 
Name Accession Description Interval E-value
PRK11649 PRK11649
putative peptidase; Provisional
 1-439 0e+00

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 980.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061   1 MQQIARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPSSAPIIKTIELEKSEIRSLLPEASEPIDQAAQEDEAI 80
Cdd:PRK11649   1 MQQIARSIALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPESAPIVKTIELEKSEIRSLLPEASEPIDQAAQEDEAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  81 PQDELDDKTENEAGIHEYVVSTGDTLSSVLNQYGIDMGNISQLAAADKDLRNLKIGQQLSWTLTADGDLQRLTWEMSRRE 160
Cdd:PRK11649  81 PQDELDDKIAGEAGVHEYVVSTGDTLSSILNQYGIDMSDISQLAAQDKELRNLKIGQQLSWTLTADGDLQRLTWEVSRRE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 161 TRTYDRTANGFKMTSEMQKGDWVNNVLKGTVGASFVSSARDAGLTSGEISSVIKAMQWQMDFRKLKKGDEFSVLMSREML 240
Cdd:PRK11649 161 TRTYDRTGNGFKETSEMQQGEWVNSVLKGTVGGSFVASAKNAGLTSAEISAVIKALQWQMDFRKLKKGDEFSVLMSREML 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 241 DGKREQSQLLGVRLRSEGKDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKQFRVSSNFNPRRLNPVTGRVAPHRGVDFAM 320
Cdd:PRK11649 241 DGKSEQSQLLGVRLRSGGKDYYAIRAEDGKFYDRNGSGLAKGFLRFPTAKQFRISSNFNPRRLNPVTGRVAPHRGVDFAM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 321 PQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGPHLHYEVWIN 400
Cdd:PRK11649 321 PVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHYEVWIN 400

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 695706061 401 QQAVNPLTAKLPRTEGLTGKDRTDYLAQVKEVIPQLSLN 439
Cdd:PRK11649 401 QQAVNPLTAKLPRTEGLTGKDRREYLAQVKEVVPQLRFD 439
Csd3_N2 pfam19425
Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This ...
 179-300 4.11e-86

Csd3 second domain; This entry represents the second domain from the Csd3 peptidase. This domain has a similar structure to pfam18059 despite low sequence similarity.


Pssm-ID: 437257 [Multi-domain]  Cd Length: 122  Bit Score: 258.49  E-value: 4.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  179 KGDWVNNVLKGTVGASFVSSARDAGLTSGEISSVIKAMQWQMDFRKLKKGDEFSVLMSREMLDGKREQSQLLGVRLRSEG 258
Cdd:pfam19425   1 EGEWQNSVLKGRVDGSFVASARKAGLTSNEISAVIKALQWQLDFRKLKKGDKFSVLMSREMLDGKREQSQLLGVRLRSGG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 695706061  259 KDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKQFRVSSNFNP 300
Cdd:pfam19425  81 KDYYAIRAEDGKFYDRNGSGLARGFLRFPTAKQFRVSSNFNP 122
OapA COG3061
Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell ...
 12-422 7.32e-63

Cell division protein YtfB/OapA (opacity-associated protein A) [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442295 [Multi-domain]  Cd Length: 425  Bit Score: 209.14  E-value: 7.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  12 FNNLPRPHRVMLGSLTVLTLaVAVWRPYVYHPSSAPIIKTIELEkSEIRSLLPEASEPIDQAAQEDEAipqdelddkten 91
Cdd:COG3061    4 MNPLPRKHRRLLGLLSALLL-LALLLPSPDASASRVSQPLVPLA-LTAEADAPAAAAPAAPAAPEGEW------------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  92 eagiHEYVVSTGDTLSSVLNQYGIDMGNISQLAAAD---KDLRNLKIGQQLSWTLTADGDLQRLTWEMSRRETRTYDRTA 168
Cdd:COG3061   70 ----QEYTVQSGDTLSQIFRRLGLSASDLYALLAAEgdaKPLSRLKPGQELRFQLDADGQLQALRYEVSRLETLLFTRQG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 169 NGFKMTSEMqkgdwvnnvlkGTVGASFVSSARDAGLTSGEISSVIKAMQWQMDFRKLKKGDEFSVLMSREMLDGKREQSQ 248
Cdd:COG3061  146 DGFQRKRVT-----------ELSDGSFSADAALASLETLELAAAAGILSDFIAAALDAGAGDAGLVELEIILDDDIDFAD 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 249 LLGVRLRSEGKDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKQFRVSSNFNPRRLNP----------------------- 305
Cdd:COG3061  215 LLFAADRFTGDYFRVYAEGEGGDGGYIGAGGFRAAKFRRRAVRFRRSSSSSSYRRRPhrlsrrrrlrrgpdaaapsgssn 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 306 --------VTGRVAPHRGVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGD 377
Cdd:COG3061  295 aagggghkITRRGGGGGGAAVGVGTGTPTTGAGLGVVRGGRGGGGGVVVGQIGRGGTYGGTGLHLHKHGHKGGGVVGQGV 374

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 695706061 378 RIAISGNTGRSTGPHLHYEVWINQQAVNPLTAKLPRTEGLTGKDR 422
Cdd:COG3061  375 TIGTLGGTGPTTGPHLHYEFVQNGVRVAPLTVKLPAAPPLAAAAA 419
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 263-408 2.87e-59

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 192.50  E-value: 2.87e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 263 AIRAEDGKFYDRSGTGLAKGFLRFPTakQFRVSSNFNPRRlNPVTGRVAPHRGVDFAMPQGTPVLAVGDGEVVVAKRSGA 342
Cdd:COG0739   50 SAAASAAAAAAAAAAAIALGSGAWPV--KGRITSGFGYRR-HPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGG 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 695706061 343 AGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGPHLHYEVWINQQAVNPLT 408
Cdd:COG0739  127 YGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLP 192
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 312-406 4.15e-47

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 156.94  E-value: 4.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  312 PHRGVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGP 391
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGP 81

                          90
                  ....*....|....*
gi 695706061  392 HLHYEVWINQQAVNP 406
Cdd:pfam01551  82 HLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 313-397 1.59e-42

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 144.66  E-value: 1.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 313 HRGVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGPH 392
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPH 80


                 ....*
gi 695706061 393 LHYEV 397
Cdd:cd12797   81 LHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 293-408 6.94e-35

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 128.22  E-value: 6.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 293 RVSSNFNPR-RLNPVTGRVAPHRGVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLR-KLLVKPG 370
Cdd:COG5821   76 KITREFGEDlVYSKTLNEWRTHTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTVYANLDsKIKVKVG 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 695706061 371 QKVKRGDRIAISGNTGR---STGPHLHYEVWINQQAVNPLT 408
Cdd:COG5821  156 QKVKKGQVIGKVGSTALfesSEGPHLHFEVLKNGKPVDPMK 196
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 237-407 9.82e-31

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 121.79  E-value: 9.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 237 REMLDGKREQSQllgvRLRSEGKDYYAIRAEDGKFYDRSGTGLAKGFLRFPTAKqfRVSSNFNPRRLNPVTgrvapHRGV 316
Cdd:COG4942  212 AAELAELQQEAE----ELEALIARLEAEAAAAAERTPAAGFAALKGKLPWPVSG--RVVRRFGERDGGGGR-----NKGI 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 317 DFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRSTGPHLHYE 396
Cdd:COG4942  281 DIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFE 360

                        170
                 ....*....|.
gi 695706061 397 VWINQQAVNPL 407
Cdd:COG4942  361 LRKNGKPVDPL 371
SpoIIQ COG5820
Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell ...
 312-408 1.52e-19

Stage II sporulation protein SpoIIQ, required for engulfement [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444522 [Multi-domain]  Cd Length: 224  Bit Score: 86.90  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 312 PHRGVDFAMPQGTP--VLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNT--GR 387
Cdd:COG5820  119 PSTGIDIAAKDGESfdVLAALSGTVTEVEEDPLLGYVVEIKHDNGVSTVYQSLSDVKVKAGDEVKQGQVIGTAGRNlfNK 198

                         90       100
                 ....*....|....*....|.
gi 695706061 388 STGPHLHYEVWINQQAVNPLT 408
Cdd:COG5820  199 DAGVHLHFEVRKDGKAVNPES 219
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 305-406 1.62e-13

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 69.25  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 305 PVTGRVAP-----HRGVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRI 379
Cdd:COG5833  107 PVSGKVVEsfqenGKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKI 186

                         90       100
                 ....*....|....*....|....*..
gi 695706061 380 AISGNTGRSTGpHLHYEVWINQQAVNP 406
Cdd:COG5833  187 GTVPATEGEEG-TFYFAIKKGGKFIDP 212
nlpD PRK10871
murein hydrolase activator NlpD;
314-407 3.90e-11

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 63.70  E-value: 3.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 314 RGVDFAMPQGTPVLAVGDGEVVVAkrsGAA--GY--YVAVRHGRTYTTRYMHLRKLLVKPGQKVKRGDRIAISGNTGRST 389
Cdd:PRK10871 220 KGIDIAGSKGQAIIATADGRVVYA---GNAlrGYgnLIIIKHNDDYLSAYAHNDTMLVREQQEVKAGQKIATMGSTGTSS 296

                         90
                 ....*....|....*...
gi 695706061 390 gPHLHYEVWINQQAVNPL 407
Cdd:PRK10871 297 -TRLHFEIRYKGKSVNPL 313
PRK11637 PRK11637
AmiB activator; Provisional
 305-407 6.27e-10

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 60.86  E-value: 6.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061 305 PVTGRVApHR------------GVDFAMPQGTPVLAVGDGEVVVAKRSGAAGYYVAVRHGRTYTTRYMHLRKLLVKPGQK 372
Cdd:PRK11637 310 PVRGPTL-HRfgeqlqgelrwkGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQ 388

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 695706061 373 VKRGDRIAISGNTGRSTGPHLHYEVWINQQAVNPL 407
Cdd:PRK11637 389 VRAGQPIALVGSSGGQGRPSLYFEIRRQGQAVNPQ 423
PRK06148 PRK06148
hypothetical protein; Provisional
 305-397 4.01e-09

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 58.88  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061  305 PVTGRVAPHRGVDFAMPQGTPVLAVGDGEVV-VAKRSGAAGY--YVAVRH----GRTYTTRYMHLRKLLV---KPGQKVK 374
Cdd:PRK06148  433 IEGERRTVHLGVDLFAPAGTPVYAPLAGTVRsVEIEAVPLGYggLVALEHetpgGDPFYTLYGHLAHEAVsrlKPGDRLA 512

                          90       100
                  ....*....|....*....|....*
gi 695706061  375 RGDRIAISGNTGRSTG--PHLHYEV 397
Cdd:PRK06148  513 AGELFGAMGDAHENGGwaPHLHFQL 537
OapA pfam04225
Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the ...
 96-170 3.78e-06

Opacity-associated protein A LysM-like domain; The OapA domain gets its name from the Haemophilus influenzae protein OapA, which is required for the expression of colony opacity, thus opacity- associated protein A. The OapA protein is required for efficient nasopharyngeal mucosal colonization, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhibits high-frequency phase variation. The OapA domain has been shown to bind to peptidoglycan in the E. coli protein YtfB. A screen to identify factors that affect cell division in E. coli discovered that overproducing a fragment of YtfB, including its OapA domain, caused cells to grow as long filaments. OapA domains are commonly associated with other domains that are involved in breaking peptidoglycan cross-links. The OapA domain is distantly related to pfam01476.


Pssm-ID: 427799 [Multi-domain]  Cd Length: 85  Bit Score: 44.65  E-value: 3.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 695706061   96 HEYVVSTGDTLSSVLNQYGIDMGNISQLAA---ADKDLRNLKIGQQLSWTLTADGDLQRLTWEMSRRETRtYDRTANG 170
Cdd:pfam04225   3 KTYTVPKGDTLAQLFRDNNLPISDVNAMAKvegADKPLSNIKSGQLVRIKLNAQGRVDELQIENGAKSVM-FFRQSDG 79
LysM smart00257
Lysin motif;
97-141 1.21e-05

Lysin motif;


Pssm-ID: 197609 [Multi-domain]  Cd Length: 44  Bit Score: 42.05  E-value: 1.21e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 695706061    97 EYVVSTGDTLSSVLNQYGIDMgniSQLAAADKDL--RNLKIGQQLSW 141
Cdd:smart00257   1 TYTVKKGDTLSSIARRYGISV---SDLLELNNILdpDNLQVGQKLKI 44
OapA_N pfam08525
Opacity-associated protein A N-terminal motif; This family includes the Haemophilus influenzae ...
 12-36 2.35e-05

Opacity-associated protein A N-terminal motif; This family includes the Haemophilus influenzae opacity-associated protein. This protein is required for efficient nasopharyngeal mucosal colonization, and its expression is associated with a distinctive transparent colony phenotype. OapA is thought to be a secreted protein, and its expression exhibits high-frequency phase variation. This motif occurs at the N-terminus of these proteins. It contains a conserved histidine followed by a run of hydrophobic residues.


Pssm-ID: 430054  Cd Length: 27  Bit Score: 40.77  E-value: 2.35e-05
                          10        20
                  ....*....|....*....|....*
gi 695706061   12 FNNLPRPHRVMLGSLTVLTLAVAVW 36
Cdd:pfam08525   2 FKPLPKLHRRLLLALSLVVLILLLW 26
LysM pfam01476
LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety ...
 98-142 4.81e-05

LysM domain; The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.


Pssm-ID: 396179 [Multi-domain]  Cd Length: 43  Bit Score: 40.46  E-value: 4.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 695706061   98 YVVSTGDTLSSVLNQYGIDMGNIsqLAAADKDLRNLKIGQQLSWT 142
Cdd:pfam01476   1 YTVKKGDTLSSIAKRYGITVEQL--AELNGLSSPNLYVGQKLKIP 43
LysM cd00118
Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain ...
 98-139 2.40e-04

Lysin Motif is a small domain involved in binding peptidoglycan; LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.


Pssm-ID: 212030 [Multi-domain]  Cd Length: 45  Bit Score: 38.62  E-value: 2.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 695706061  98 YVVSTGDTLSSVLNQYGIDmgnISQLAAA--DKDLRNLKIGQQL 139
Cdd:cd00118    3 YTVKPGDTLWSIAKKYGVT---VEELAAAnpLINPDCIYPGQKL 43
LysM COG1388
LysM repeat [Cell wall/membrane/envelope biogenesis];
4-139 1.40e-03

LysM repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440998 [Multi-domain]  Cd Length: 156  Bit Score: 39.31  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695706061   4 IARSVALAFNNLPRPHRVMLGSLTVLTLAVAVWRPYVYHPSSAPIIKTIELEKSEIRSLLPEASEPIDQAAQEDEAIPQD 83
Cdd:COG1388   13 LAAVLTLLAALLLLAAALAAVALLLLAALAPAGLSLAAALNGEALLLLLPAAAAAAKAALAAAPEAAAAAAARYTVKSGD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695706061  84 ELDD-----KTENEAGIHEYVVSTGDTLSSVLNQYGIDmgnISQLAAADKdLRN--LKIGQQL 139
Cdd:COG1388   93 TLSGiarryGAAAAPSPVTYTVKKGDTLWSIARRYGVS---VEELKRWNG-LSSdtIRPGQKL 151
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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