ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];

                        10        20
                ....*....|....*....|
gi 17537511  88 VISAIGPQGAGKSTLLSMLA 107
Cdd:COG4604  29 ITALIGPNGAGKSTLLSMIS 48

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 17537511  85 NFNVISAIGPQGAGKSTLLSMLAGnnsrqmyREYVFRpvsreanEQSRHQTIQIDIYIVNHQIFLDCQPMYSFSIM--EG 162
Cdd:cd01851   6 PVVVVSVFGSQSSGKSFLLNHLFG-------TSDGFD-------VMDTSQQTTKGIWMWSDPFKDTDGKKHAVLLLdtEG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537511 163 LpkvrGGRfdDSTAMSDTLRLTAFLLYVSHTVLVVS-----ETHYDKVIIDTLRVAEQIRPYLAIFRPKlaidRKTNLVF 237
Cdd:cd01851  72 T----DGR--ERGEFENDARLFALATLLSSVLIYNMwqtilGDDLDKLMGLLKTALETLGLAGLHNFSK----PKPLLLF 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17537511 238 -IKTKASSIDLAPTVIREREELLRLSFQDSRWLKVSQEPFKTLIVLEEIRVRREHLFEEGDEPDEAaslNEFDEQIAELR 316
Cdd:cd01851 142 vVRDFTGPTPLEGLDVTEKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQNDGRLKDLP---PEFRKALKALR 218

                ....*.
gi 17537511 317 EELQKN 322
Cdd:cd01851 219 QRFFSS 224

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];

                        10        20
                ....*....|....*....|
gi 17537511  88 VISAIGPQGAGKSTLLSMLA 107
Cdd:COG4604  29 ITALIGPNGAGKSTLLSMIS 48

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.

                        10        20
                ....*....|....*....|.
gi 17537511  88 VISAIGPQGAGKSTLLSMLAG 108
Cdd:cd03214  27 IVGILGPNGAGKSTLLKTLAG 47

vitamin B12-transporter ATPase; Provisional

                         10
                 ....*....|....*..
gi 17537511   92 IGPQGAGKSTLLSMLAG 108
Cdd:PRK03695  28 VGPNGAGKSTLLARMAG 44

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];

                        10        20
                ....*....|....*....|
gi 17537511  88 VISAIGPQGAGKSTLLSMLA 107
Cdd:COG4604  29 ITALIGPNGAGKSTLLSMIS 48

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];

                        10
                ....*....|....*..
gi 17537511  92 IGPQGAGKSTLLSMLAG 108
Cdd:COG4138  28 IGPNGAGKSTLLARMAG 44

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.

                        10        20
                ....*....|....*....|.
gi 17537511  88 VISAIGPQGAGKSTLLSMLAG 108
Cdd:cd03214  27 IVGILGPNGAGKSTLLKTLAG 47

vitamin B12-transporter ATPase; Provisional

                         10
                 ....*....|....*..
gi 17537511   92 IGPQGAGKSTLLSMLAG 108
Cdd:PRK03695  28 VGPNGAGKSTLLARMAG 44

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];

                        10
                ....*....|....*..
gi 17537511  92 IGPQGAGKSTLLSMLAG 108
Cdd:COG4559  33 IGPNGAGKSTLLKLLTG 49

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                        10        20
                ....*....|....*....|....*....
gi 17537511  85 NFNV-----ISAIGPQGAGKSTLLSMLAG 108
Cdd:cd03293  24 SLSVeegefVALVGPSGCGKSTLLRIIAG 52

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                        10
                ....*....|....*..
gi 17537511  92 IGPQGAGKSTLLSMLAG 108
Cdd:cd03230  32 LGPNGAGKTTLIKIILG 48