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 1893045331 252 VDFRRVWSGRTEYgTDwwQAIEGSHTLVAGSTGAGKNSLTWAPIISMAPAIRDGLVRVSGIDPKGMELAYGRRVFHRY-- 329
Cdd:pfam01580  19 IALGKDISGNPEV-FD--LKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLsv 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1893045331 330 --ASTSKDALALLDDLIDGMTARKERFSTHKR 359
Cdd:pfam01580  96 pvATDPKRALRALEWLVDEMERRYALFRALGV 127

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893045331 252 VDFRRVWSGRTEYgTDwwQAIEGSHTLVAGSTGAGKNSLTWAPIISMAPAIRDGLVRVSGIDPKGMELAYGRRVFHRY-- 329
Cdd:pfam01580  19 IALGKDISGNPEV-FD--LKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLsv 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1893045331 330 --ASTSKDALALLDDLIDGMTARKERFSTHKR 359
Cdd:pfam01580  96 pvATDPKRALRALEWLVDEMERRYALFRALGV 127

FtsK/SpoIIIE family; FtsK has extensive sequence similarity to wide variety of proteins from prokaryotes and plasmids, termed the FtsK/SpoIIIE family. This domain contains a putative ATP binding P-loop motif. It is found in the FtsK cell division protein from E. coli and the stage III sporulation protein E SpoIIIE, which has roles in regulation of prespore specific gene expression in B. subtilis. A mutation in FtsK causes a temperature sensitive block in cell division and it is involved in peptidoglycan synthesis or modification. The SpoIIIE protein is implicated in intercellular chromosomal DNA transfer.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893045331 252 VDFRRVWSGRTEYgTDwwQAIEGSHTLVAGSTGAGKNSLTWAPIISMAPAIRDGLVRVSGIDPKGMELAYGRRVFHRY-- 329
Cdd:pfam01580  19 IALGKDISGNPEV-FD--LKKMPVHLLIAGATGSGKSVALNTLILSLAYMHTPEEVQLYCIDPKMGELSAYEDIPHLLsv 95

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1893045331 330 --ASTSKDALALLDDLIDGMTARKERFSTHKR 359
Cdd:pfam01580  96 pvATDPKRALRALEWLVDEMERRYALFRALGV 127