PSTB_MYCGE
ID PSTB_MYCGE Reviewed; 329 AA.
AC P47650; Q49513;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000255|HAMAP-Rule:MF_01702};
DE EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=ABC phosphate transporter {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=Phosphate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01702};
GN Name=pstB {ECO:0000255|HAMAP-Rule:MF_01702}; OrderedLocusNames=MG410;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 101-313.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phosphate(out) = ADP + H(+) + 2 phosphate(in);
CC Xref=Rhea:RHEA:24440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.3.2.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01702};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (PstB),
CC two transmembrane proteins (PstC and PstA) and a solute-binding protein
CC (PstS). {ECO:0000255|HAMAP-Rule:MF_01702}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01702};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01702}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate
CC importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L43967; AAC71638.1; -; Genomic_DNA.
DR EMBL; U01707; AAB01019.1; -; Genomic_DNA.
DR PIR; D64245; D64245.
DR RefSeq; WP_009885613.1; NZ_AAGX01000001.1.
DR AlphaFoldDB; P47650; -.
DR SMR; P47650; -.
DR STRING; 243273.MG_410; -.
DR EnsemblBacteria; AAC71638; AAC71638; MG_410.
DR KEGG; mge:MG_410; -.
DR eggNOG; COG1117; Bacteria.
DR HOGENOM; CLU_000604_1_22_14; -.
DR OMA; TIDICRV; -.
DR OrthoDB; 1416748at2; -.
DR BioCyc; MGEN243273:G1GJ2-507-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015415; F:ATPase-coupled phosphate ion transmembrane transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR CDD; cd03260; ABC_PstB_phosphate_transporter; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005670; Phosp_transpt1.
DR PANTHER; PTHR43423; PTHR43423; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00972; 3a0107s01c2; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51238; PSTB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Phosphate transport; Reference proteome; Translocase; Transport.
FT CHAIN 1..329
FT /note="Phosphate import ATP-binding protein PstB"
FT /id="PRO_0000092840"
FT DOMAIN 83..325
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT BINDING 116..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT CONFLICT 310..329
FT /note="KQIFTKPKQKATNSYISGKN -> NRYL (in Ref. 2; AAB01019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 37940 MW; C021505065B933D3 CRC64;
MEKNIKALWK NFQLKLEKIK HYRKLYEQQI KEYKKKITGL NNETDANEIS RIKNEIEILN
RLIKIKNTKD NVIKKDFDEK NVFEIRNFNF WYNKNKQVLF DINLDIKRNK ITALIGKSGC
GKSTFIRCLN KLNDLNENTR WTGDIYFLGK NINSGIINDL TLRTSVGMVF QKLTPFNFSI
FENIAYGIRA HGIHNKNAIN EIVRQALISA ALWDEVKDNL HRNANTLSGG QQQRLCIARA
IALQPDVLLM DEPTSALDSI ATNSIELLIQ QLKEKFTIVI VTHSMAQTIR ITDETIFFAD
GRVIEQGTTK QIFTKPKQKA TNSYISGKN
