sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2743942939   2 YALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK11650   85 YALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR 142

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:TIGR01187  50 SYALFPHMTVEENVAFGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQR 108

ribosome-associated ATPase/putative transporter RbbA;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2743942939   4 LYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQ 58
Cdd:NF033858   89 LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQ 143

zinc ABC transporter ATP-binding protein AztA;

                          10        20        30
                  ....*....|....*....|....*....|
gi 2743942939  30 RRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:NF040873   98 AAVDDALERVGLADLAGRQLGELSGGQRQR 127

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2743942939   2 YALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK11650   85 YALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR 142

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03301    80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQR 138

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. 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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03300    80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQR 138

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG1116    88 EPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQR 146

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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03293    81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQR 139

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:TIGR01187  50 SYALFPHMTVEENVAFGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQR 108

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2743942939   2 YALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03299    80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQR 137

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2743942939   4 LYPHMSVRKNIAFPMRmAGLSKDEQDR-RIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG3840    82 LFPHLTVAQNIGLGLR-PGLKLTAEQRaQVEQALERVGLAGLLDRLPGQLSGGQRQR 137

ferric ABC transporter ATP-binding protein;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK11432   86 SYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQR 144

putrescine ABC transporter ATP-binding subunit PotG;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK11607   99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQR 157

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2743942939   9 SVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG1122    92 TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQR 142

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). 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        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2743942939   2 YALYPHMSVRKNIAFPMRM----AGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03296    83 YALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQR 144

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. 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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2743942939   2 YALYPHMSVRKNIAFPMRMAGLSKDEQdrRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03297    84 YALFPHLNVRENLAFGLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQR 139

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   3 ALYPHMSVRKNIAFPMRMAG-LSKDEQDRRIEAAAKALNL-TNYLDRRPGQLSGGQRQR 59
Cdd:COG1123   354 SLNPRMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQR 412

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2743942939  10 VRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG1135    99 VAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR 148

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2743942939   4 LYPHMSVRKNIAFPMRmAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG4136    87 LFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRAR 141

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743942939   1 SYALYPHMSVRKNIAF-PMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03262    84 QFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR 143

ATP-binding cassette transport system involved in resistance to organic solvents; 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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2743942939   3 ALYPHMSVRKNIAFPMRMAG-LSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03261    87 ALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKR 144

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2743942939   3 ALYPHMSVRKNIAFPMRM-AGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG1127    92 ALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR 149

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. 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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2743942939   5 YPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03264    84 YPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRR 138

ribosome-associated ATPase/putative transporter RbbA;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2743942939   4 LYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQ 58
Cdd:NF033858   89 LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQ 143

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03266    86 STGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQK 144

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743942939   3 ALYPHMSVRKNIAFPMRMAG-LSKDEQDRRIEAAA-KALNL-TNYLDRRPGQLSGGQRQR 59
Cdd:cd03257    94 SLNPRMTIGEQIAEPLRIHGkLSKKEARKEAVLLLlVGVGLpEEVLNRYPHELSGGQRQR 153

DL-methionine transporter ATP-binding subunit; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2743942939  13 NIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK11153  102 NVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR 148

proline/glycine betaine ABC transporter ATP-binding protein ProV;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   1 SYALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK10070  114 SFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQR 172

macrolide ABC transporter ATP-binding protein/permease MacB;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2743942939   2 YALYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK10535   95 YHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQR 152

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2743942939   3 ALYPHMSVRKNIAFPMRM-AGLSKDEQDRRIEAAAKALNLTN---YLDRRPGQLSGGQRQR 59
Cdd:COG0444    98 SLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158

nickel ABC transporter ATP-binding protein NikE;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2743942939   3 ALYPHMSVRKNIAFPMR-MAGLSKDEQDRRIEAAAKALNLT-NYLDRRPGQLSGGQRQR 59
Cdd:PRK10419  101 AVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159

glutamine ABC transporter ATP-binding protein GlnQ;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2743942939   4 LYPHMSVRKNIAF-PMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK09493   88 LFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQR 144

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2743942939   7 HMSVRKNIAFPMRMAG-LSKDEQDRRIEAAAKALNLTNYLDRR--PGQLSGGQRQR 59
Cdd:cd03260    94 PGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDRlhALGLSGGQQQR 149

cobalt transporter ATP-binding subunit; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2743942939   9 SVRKNIAF-PMRMaGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK13639   95 TVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR 145

energy-coupling factor transporter ATPase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2743942939   9 SVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLT--NYLDRRPGQLSGGQRQR 59
Cdd:PRK13637  100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRR 152

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2743942939   4 LYPHMSVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03292    89 LLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQR 144

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2743942939  18 MRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:cd03235    99 KGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQR 140

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2743942939   7 HMSVRKNIAFPMRMAGLSKDEQdrRIEAAAKALNLTN-YLDRRPGQLSGGQRQR 59
Cdd:COG4619    87 GGTVRDNLPFPFQLRERKFDRE--RALELLERLGLPPdILDKPVERLSGGERQR 138

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2743942939   5 YPHMSvrkniafpmRMAGLSKDEqDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG1120   101 YPHLG---------LFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQR 145

energy-coupling factor transporter ATPase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2743942939   9 SVRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK13650   98 TVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR 148

cobalt transporter ATP-binding subunit; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2743942939   9 SVRKNIAF-PMRMaGLSKDEQDRRieaAAKALNLT----NYLDRRPGQLSGGQRQR 59
Cdd:PRK13651  122 TIEKDIIFgPVSM-GVSKEEAKKR---AAKYIELVgldeSYLQRSPFELSGGQKRR 173

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2743942939   7 HMSVRKNIAFpmrmaGlSKDEQDRRIEAAAKALNLTNYLDRRPG-----------QLSGGQRQR 59
Cdd:COG1132   427 SGTIRENIRY-----G-RPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQR 484

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

                          10        20        30
                  ....*....|....*....|....*....|....
gi 2743942939  27 EQDRR-IEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:COG4604   110 AEDREiIDEAIAYLDLEDLADRYLDELSGGQRQR 143

energy-coupling factor transporter ATPase;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2743942939  10 VRKNIAFPMRMAGLSKDEQDRRIEAAAKALNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK13633  103 VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR 152

molybdenum ABC transporter ATP-binding protein ModC;

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2743942939   4 LYPHMSVRKNIAFPMrmAGLSKDEQDRRIEAaakaLNLTNYLDRRPGQLSGGQRQR 59
Cdd:PRK11144   87 LFPHYKVRGNLRYGM--AKSMVAQFDKIVAL----LGIEPLLDRYPGSLSGGEKQR 136