P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487409177  40 GIMGKSGAGKSSLCNALFQGEVTPVSAlmtVLPGHAAIHLMtRLQDELRTESV--------RTQTREQFTGAVDRIFDTA 111
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGD---RRPTTRAAQAY-VWQTGGDGLVLldlpgvgeRGRRDREYEELYRRLLPEA 76

                 ...
gi 487409177 112 ESV 114
Cdd:cd11383   77 DLV 79

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487409177  40 GIMGKSGAGKSSLCNALFQGEVTPVSAlmtVLPGHAAIHLMtRLQDELRTESV--------RTQTREQFTGAVDRIFDTA 111
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGD---RRPTTRAAQAY-VWQTGGDGLVLldlpgvgeRGRRDREYEELYRRLLPEA 76

                 ...
gi 487409177 112 ESV 114
Cdd:cd11383   77 DLV 79

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.

                          10        20
                  ....*....|....*....|....*..
gi 487409177   39 IGIMGKSGAGKSSLCNALFqGEVTPVS 65
Cdd:pfam01926   2 VALVGRPNVGKSTLINALT-GAKAIVS 27

YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487409177  40 GIMGKSGAGKSSLCNALFQGEVTPVSAlmtVLPGHAAIHLMtRLQDELRTESV--------RTQTREQFTGAVDRIFDTA 111
Cdd:cd11383    1 GLMGKTGAGKSSLCNALFGTEVAAVGD---RRPTTRAAQAY-VWQTGGDGLVLldlpgvgeRGRRDREYEELYRRLLPEA 76

                 ...
gi 487409177 112 ESV 114
Cdd:cd11383   77 DLV 79

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.

                          10        20
                  ....*....|....*....|....*..
gi 487409177   39 IGIMGKSGAGKSSLCNALFqGEVTPVS 65
Cdd:pfam01926   2 VALVGRPNVGKSTLINALT-GAKAIVS 27

ABC transporter C family member; Provisional

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487409177    3 PSDAIEAIE--KPLSSLPYPISRHILE-HLRKLTSHEPV-------------IGIMGKSGAGKSSLCNALFQ 58
Cdd:PLN03232 1213 PSEATAIIEnnRPVSGWPSRGSIKFEDvHLRYRPGLPPVlhglsffvspsekVGVVGRTGAGKSSMLNALFR 1284

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487409177    2 NPSDAIEAIEKPLSSLPYPI------SRHILEHLRK-LTSHepVIGIMGKSGAGKSSLCNAL 56
Cdd:pfam03193  67 DEEEELEELLKIYRAIGYPVlfvsakTGEGIEALKElLKGK--TTVLAGQSGVGKSTLLNAL 126

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 487409177   6 AIEAIEKPLSSlPYPISRHILEHLRKLTSHEPVIGIMGKSGAGKSSLCNAL 56
Cdd:cd03114   17 AITLVESGRPD-HRELAQELLDALLPQAGRAFRVGITGPPGAGKSTLIEAL 66

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.

                         10        20
                 ....*....|....*....|....*....
gi 487409177  40 GIMGKSGAGKSSLCNALFQGEVTPVSALM 68
Cdd:cd00880    1 AIFGRPNVGKSSLLNALLGQNVGIVSPIP 29

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487409177   3 PSDAIEAIEKPLSSLPYP---ISRH-------ILEHLRKLTShepviGIMGKSGAGKSSLCNALFQGEV 61
Cdd:cd01854   47 DDEELEELLEIYEKLGYPvlaVSAKtgegldeLRELLKGKTS-----VLVGQSGVGKSTLLNALLPELV 110