PSTB1_MYCTU
ID PSTB1_MYCTU Reviewed; 258 AA.
AC P9WQL1; L0T7L4; O53832;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Phosphate import ATP-binding protein PstB 1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE EC=7.3.2.1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=ABC phosphate transporter 1 {ECO:0000255|HAMAP-Rule:MF_01702};
DE AltName: Full=Phosphate-transporting ATPase 1 {ECO:0000255|HAMAP-Rule:MF_01702};
GN Name=pstB1 {ECO:0000255|HAMAP-Rule:MF_01702}; Synonyms=phoT;
GN OrderedLocusNames=Rv0820; ORFNames=MTV043.12;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, AND INDUCTION BY PHOSPHATE STARVATION.
RC STRAIN=H37Rv;
RX PubMed=20933472; DOI=10.1016/j.tube.2010.09.004;
RA Vanzembergh F., Peirs P., Lefevre P., Celio N., Mathys V., Content J.,
RA Kalai M.;
RT "Effect of PstS sub-units or PknD deficiency on the survival of
RT Mycobacterium tuberculosis.";
RL Tuberculosis 90:338-345(2010).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import (Probable). Responsible for energy coupling to the
CC transport system. {ECO:0000255|HAMAP-Rule:MF_01702,
CC ECO:0000305|PubMed:20933472}.
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 -!- INDUCTION: Transcription induced by phosphate starvation, no change in
CC protein levels on phosphate starvation (at protein level). If bacteria
CC are starved prior to growth in phosphate-free medium protein expression
CC disappears. {ECO:0000269|PubMed:20933472}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate
CC importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}.
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DR EMBL; AL123456; CCP43568.1; -; Genomic_DNA.
DR PIR; D70810; D70810.
DR RefSeq; NP_215335.1; NC_000962.3.
DR RefSeq; WP_003404312.1; NZ_NVQJ01000066.1.
DR AlphaFoldDB; P9WQL1; -.
DR SMR; P9WQL1; -.
DR STRING; 83332.Rv0820; -.
DR PaxDb; P9WQL1; -.
DR DNASU; 885136; -.
DR GeneID; 885136; -.
DR KEGG; mtu:Rv0820; -.
DR TubercuList; Rv0820; -.
DR eggNOG; COG1117; Bacteria.
DR OMA; TIDICRV; -.
DR PhylomeDB; P9WQL1; -.
DR Proteomes; UP000001584; 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 GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Phosphate transport; Reference proteome; Translocase; Transport.
FT CHAIN 1..258
FT /note="Phosphate import ATP-binding protein PstB 1"
FT /id="PRO_0000092849"
FT DOMAIN 5..247
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01702"
SQ SEQUENCE 258 AA; 28061 MW; F15294F2730CD75B CRC64;
MAKRLDLTDV NIYYGSFHAV ADVSLAILPR SVTAFIGPSG CGKTTVLRTL NRMHEVIPGA
RVEGAVLLDD QDIYAPGIDP VGVRRAIGMV FQRPNPFPAM SIRNNVVAGL KLQGVRNRKV
LDDTAESSLR GANLWDEVKD RLDKPGGGLS GGQQQRLCIA RAIAVQPDVL LMDEPCSSLD
PISTMAIEDL ISELKQQYTI VIVTHNMQQA ARVSDQTAFF NLEAVGKPGR LVEIASTEKI
FSNPNQKATE DYISGRFG
