NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501406594|ref|WP_012438160|]
View 

MULTISPECIES: M23 family metallopeptidase [Xanthomonas]

Protein Classification

M23 family metallopeptidase( domain architecture ID 11432770)

M23 family metallopeptidase lyses bacterial cell wall peptidoglycans

EC:  3.4.24.-
Gene Ontology:  GO:0046872|GO:0008237
MEROPS:  M23
PubMed:  36386627

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 83-277 4.18e-46

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: 153.59  E-value: 4.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594  83 LQVQITRADGGKETATIAVTPRDWPVERVNGVPPKTVNPPPAIAERIKREQAQVTAARDRDDPRADFAQPFVWPVQGRIS 162
Cdd:COG0739    1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 163 GRFGNARVYNGQPGAGHSGMDIAVPTGTPVKAPAAGVVTFAAPDLYLTGGTLLlDHGFGISSNFLHLSRIDVKVGDRVEQ 242
Cdd:COG0739   81 SGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVII-DHGNGYTTLYAHLSSILVKVGQRVKA 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 501406594 243 GQVIAAVGATGRATGPHLHWGMNWFDVRIDPLLVL 277
Cdd:COG0739  160 GQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
class_II_aaRS-like_core super family cl00268
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 51-93 2.92e-03

Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.


The actual alignment was detected with superfamily member PRK02983:

Pssm-ID: 444800 [Multi-domain]  Cd Length: 1094  Bit Score: 39.18  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 501406594   51 PAGSRVEYAGRALRVSGYGSVVFGIGRDATGPLQVQITRADGG 93
Cdd:PRK02983  649 PTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLE 691
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 83-277 4.18e-46

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: 153.59  E-value: 4.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594  83 LQVQITRADGGKETATIAVTPRDWPVERVNGVPPKTVNPPPAIAERIKREQAQVTAARDRDDPRADFAQPFVWPVQGRIS 162
Cdd:COG0739    1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 163 GRFGNARVYNGQPGAGHSGMDIAVPTGTPVKAPAAGVVTFAAPDLYLTGGTLLlDHGFGISSNFLHLSRIDVKVGDRVEQ 242
Cdd:COG0739   81 SGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVII-DHGNGYTTLYAHLSSILVKVGQRVKA 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 501406594 243 GQVIAAVGATGRATGPHLHWGMNWFDVRIDPLLVL 277
Cdd:COG0739  160 GQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 178-273 1.64e-33

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: 117.65  E-value: 1.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594  178 GHSGMDIAVPTGTPVKAPAAGVVTFAAPDLYLTGGTLLlDHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGATGRATG 257
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVII-DHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 501406594  258 PHLHWGMNWFDVRIDP 273
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 179-264 7.93e-30

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: 107.68  E-value: 7.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 179 HSGMDIAVPTGTPVKAPAAGVVTFAAPDLYLTGGTLLlDHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGATGRATGP 258
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVII-DHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGP 79


                 ....*.
gi 501406594 259 HLHWGM 264
Cdd:cd12797   80 HLHFEI 85
PRK11649 PRK11649
putative peptidase; Provisional
 130-262 6.01e-15

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 74.32  E-value: 6.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 130 KREQAQVTAARDRDDP------RAD-----------FAQPFV-WPV--QGRISGRFgNARVYNGQPG--AGHSGMDIAVP 187
Cdd:PRK11649 243 KSEQSQLLGVRLRSGGkdyyaiRAEdgkfydrngsgLAKGFLrFPTakQFRISSNF-NPRRLNPVTGrvAPHRGVDFAMP 321

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501406594 188 TGTPVKAPAAGVVTFAAPDLYLTGGTLLLdHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGATGRATGPHLHW 262
Cdd:PRK11649 322 VGTPVLAVGDGEVVVAKRSGAAGNYVAIR-HGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHY 395
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
51-93 2.92e-03

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 39.18  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 501406594   51 PAGSRVEYAGRALRVSGYGSVVFGIGRDATGPLQVQITRADGG 93
Cdd:PRK02983  649 PTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLE 691
PTBA TIGR00830
PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside ...
 186-246 5.65e-03

PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside (Glc) SuperFamily. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). The IIA, IIB and IIC domains of all of the permeases listed below are demonstrably homologous. These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. The three-dimensional structures of the IIA and IIB domains of the E. coli glucose permease have been elucidated. IIAglchas a complex b-sandwich structure while IIBglc is a split ab-sandwich with a topology unrelated to the split ab-sandwich structure of HPr. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]


Pssm-ID: 273289 [Multi-domain]  Cd Length: 121  Bit Score: 36.07  E-value: 5.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501406594  186 VPTGTPVKAPAAGVVTFAAPdlyltggtllLDHGFGISSN-----FLHLSrID------------VKVGDRVEQGQVI 246
Cdd:TIGR00830  32 LPTDGKVVAPVDGKIGKIFP----------TKHAFGIESDngveiLIHIG-IDtvklngegftshVEEGDRVKKGDPL 98
 
Name Accession Description Interval E-value
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 83-277 4.18e-46

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: 153.59  E-value: 4.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594  83 LQVQITRADGGKETATIAVTPRDWPVERVNGVPPKTVNPPPAIAERIKREQAQVTAARDRDDPRADFAQPFVWPVQGRIS 162
Cdd:COG0739    1 AALALALAAALLALALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRIT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 163 GRFGNARVYNGQPGAGHSGMDIAVPTGTPVKAPAAGVVTFAAPDLYLTGGTLLlDHGFGISSNFLHLSRIDVKVGDRVEQ 242
Cdd:COG0739   81 SGFGYRRHPVTGRRRFHKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVII-DHGNGYTTLYAHLSSILVKVGQRVKA 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 501406594 243 GQVIAAVGATGRATGPHLHWGMNWFDVRIDPLLVL 277
Cdd:COG0739  160 GQVIGYVGNTGRSTGPHLHFEVRVNGKPVDPLPFL 194
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 178-273 1.64e-33

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: 117.65  E-value: 1.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594  178 GHSGMDIAVPTGTPVKAPAAGVVTFAAPDLYLTGGTLLlDHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGATGRATG 257
Cdd:pfam01551   2 FHKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVII-DHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTG 80

                          90
                  ....*....|....*.
gi 501406594  258 PHLHWGMNWFDVRIDP 273
Cdd:pfam01551  81 PHLHFEIRKNGKPVDP 96
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 125-279 1.46e-32

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: 122.95  E-value: 1.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 125 IAERIKREQAQVtAARDRDDPRADFAQP---FVWPVQGRISGRFGNARVYngqpGAGHSGMDIAVPTGTPVKAPAAGVVT 201
Cdd:COG4942  225 LEALIARLEAEA-AAAAERTPAAGFAALkgkLPWPVSGRVVRRFGERDGG----GGRNKGIDIAAPPGAPVRAVADGTVV 299

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501406594 202 FAAPDLyltggtlllDHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGATGRATGPHLHWGMNWFDVRIDPLLVLER 279
Cdd:COG4942  300 YAGWLRgygn-lviiDHGGGYLTLYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAK 376
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 179-264 7.93e-30

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: 107.68  E-value: 7.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 179 HSGMDIAVPTGTPVKAPAAGVVTFAAPDLYLTGGTLLlDHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGATGRATGP 258
Cdd:cd12797    1 HNGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVII-DHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGP 79


                 ....*.
gi 501406594 259 HLHWGM 264
Cdd:cd12797   80 HLHFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 151-274 1.92e-28

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: 107.80  E-value: 1.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 151 QPFVWPVQGRISGRFGNARVYNgqPGAG----HSGMDIAVPTGTPVKAPAAGVVTFAAPDlYLTGGTLLLDHGFGISSNF 226
Cdd:COG5821   67 NKFLKPVSGKITREFGEDLVYS--KTLNewrtHTGIDIAAKEGTPVKAAADGVVVEVGKD-PKYGITVVIDHGNGIKTVY 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501406594 227 LHL-SRIDVKVGDRVEQGQVIAAVGATGR---ATGPHLHWGMNWFDVRIDPL 274
Cdd:COG5821  144 ANLdSKIKVKVGQKVKKGQVIGKVGSTALfesSEGPHLHFEVLKNGKPVDPM 195
PRK11649 PRK11649
putative peptidase; Provisional
 130-262 6.01e-15

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 74.32  E-value: 6.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 130 KREQAQVTAARDRDDP------RAD-----------FAQPFV-WPV--QGRISGRFgNARVYNGQPG--AGHSGMDIAVP 187
Cdd:PRK11649 243 KSEQSQLLGVRLRSGGkdyyaiRAEdgkfydrngsgLAKGFLrFPTakQFRISSNF-NPRRLNPVTGrvAPHRGVDFAMP 321

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501406594 188 TGTPVKAPAAGVVTFAAPDLYLTGGTLLLdHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGATGRATGPHLHW 262
Cdd:PRK11649 322 VGTPVLAVGDGEVVVAKRSGAAGNYVAIR-HGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTGRSTGPHLHY 395
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 136-252 3.67e-10

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


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 58.46  E-value: 3.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 136 VTAARDRDDPRADFAQPFVWPVQGRISGRFGNarvyngqpgaGHSGMDIAVPTGTPVKAPAAGVVTFAAPDlYLTGGTLL 215
Cdd:COG5833   87 FLPPFGKEEETVEQGEAFALPVSGKVVESFQE----------NGKGVDIETPGGANVKAVKEGYVIFAGKD-EETGKTVI 155

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 501406594 216 LDHGFGISSNFLHLSRIDVKVGDRVEQGQVIAAVGAT 252
Cdd:COG5833  156 IQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPAT 192
PRK11637 PRK11637
AmiB activator; Provisional
 124-270 3.21e-07

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 50.85  E-value: 3.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 124 AIAERIKREQAQVtaaRDR--------------DDPRADFA------QP---FVWPVQGRISGRFGNARvyngQPGAGHS 180
Cdd:PRK11637 258 ARAEREAREAARV---RDKqkqakrkgstykptESERSLMSrtgglgRPrgqAFWPVRGPTLHRFGEQL----QGELRWK 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594 181 GMDIAVPTGTPVKAPAAGVVTFAapdlyltggtlllD------------HGFGISSNFLHLSRIDVKVGDRVEQGQVIAA 248
Cdd:PRK11637 331 GMVIGASEGTEVKAIADGRVLLA-------------DwlqgyglvvvveHGKGDMSLYGYNQSALVSVGAQVRAGQPIAL 397

                        170       180
                 ....*....|....*....|..
gi 501406594 249 VGATGRATGPHLhwgmnWFDVR 270
Cdd:PRK11637 398 VGSSGGQGRPSL-----YFEIR 414
PRK06148 PRK06148
hypothetical protein; Provisional
 179-261 9.47e-05

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 43.86  E-value: 9.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501406594  179 HSGMDIAVPTGTPVKAPAAGVVTFAA--PDLYLTGGTLLLDHGFGISSNFL----HLSRIDV---KVGDRVEQGQVIAAV 249
Cdd:PRK06148  441 HLGVDLFAPAGTPVYAPLAGTVRSVEieAVPLGYGGLVALEHETPGGDPFYtlygHLAHEAVsrlKPGDRLAAGELFGAM 520

                          90
                  ....*....|....
gi 501406594  250 GATGRATG--PHLH 261
Cdd:PRK06148  521 GDAHENGGwaPHLH 534
lysS PRK02983
bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;
51-93 2.92e-03

bifunctional lysylphosphatidylglycerol synthetase/lysine--tRNA ligase LysX;


Pssm-ID: 235095 [Multi-domain]  Cd Length: 1094  Bit Score: 39.18  E-value: 2.92e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 501406594   51 PAGSRVEYAGRALRVSGYGSVVFGIGRDATGPLQVQITRADGG 93
Cdd:PRK02983  649 PTGEEVSVSGRVLRIRDYGGVLFADLRDWSGELQVLLDASRLE 691
PTBA TIGR00830
PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside ...
 186-246 5.65e-03

PTS system, glucose subfamily, IIA component; These are part of the The PTS Glucose-Glucoside (Glc) SuperFamily. The Glc family includes permeases specific for glucose, N-acetylglucosamine and a large variety of a- and b-glucosides. However, not all b-glucoside PTS permeases are in this class, as the cellobiose (Cel) b-glucoside PTS permease is in the Lac family (TC #4.A.3). The IIA, IIB and IIC domains of all of the permeases listed below are demonstrably homologous. These permeases show limited sequence similarity with members of the Fru family (TC #4.A.2). Several of the PTS permeases in the Glc family lack their own IIA domains and instead use the glucose IIA protein (IIAglc or Crr). Most of these permeases have the B and C domains linked together in a single polypeptide chain, and a cysteyl residue in the IIB domain is phosphorylated by direct phosphoryl transfer from IIAglc(his~P). Those permeases which lack a IIA domain include the maltose (Mal), arbutin-salicin-cellobiose (ASC), trehalose (Tre), putative glucoside (Glv) and sucrose (Scr) permeases of E. coli . Most, but not all Scr permeases of other bacteria also lack a IIA domain. The three-dimensional structures of the IIA and IIB domains of the E. coli glucose permease have been elucidated. IIAglchas a complex b-sandwich structure while IIBglc is a split ab-sandwich with a topology unrelated to the split ab-sandwich structure of HPr. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]


Pssm-ID: 273289 [Multi-domain]  Cd Length: 121  Bit Score: 36.07  E-value: 5.65e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501406594  186 VPTGTPVKAPAAGVVTFAAPdlyltggtllLDHGFGISSN-----FLHLSrID------------VKVGDRVEQGQVI 246
Cdd:TIGR00830  32 LPTDGKVVAPVDGKIGKIFP----------TKHAFGIESDngveiLIHIG-IDtvklngegftshVEEGDRVKKGDPL 98
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH