PSTA2_MYCTU
ID PSTA2_MYCTU Reviewed; 301 AA.
AC P9WG09; L0T6V1; O08115; P0A626; Q50796;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Phosphate transport system permease protein PstA 2;
GN Name=pstA2; OrderedLocusNames=Rv0936; ORFNames=MTCY08D9.03c;
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 [GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=8918249; DOI=10.1016/0378-1119(96)00242-9;
RA Braibant M., Lefevre P., de Wit L., Peirs P., Ooms J., Huygen K.,
RA Andersen A.B., Content J.;
RT "A Mycobacterium tuberculosis gene cluster encoding proteins of a phosphate
RT transporter homologous to the Escherichia coli Pst system.";
RL Gene 176:171-176(1996).
RN [2]
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 [3]
RP FUNCTION, AND INDUCTION.
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 [4]
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 binding-protein-dependent transport system for
CC phosphate; probably responsible for the translocation of the substrate
CC across the membrane. {ECO:0000305|PubMed:20933472}.
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Transcription slightly induced by phosphate starvation, part
CC of the pstB3-pstS2-pstC1-pstA2 operon (PubMed:20933472).
CC {ECO:0000269|PubMed:20933472}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; Z68202; CAA92397.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43684.1; -; Genomic_DNA.
DR PIR; H70584; H70584.
DR RefSeq; NP_215451.1; NC_000962.3.
DR RefSeq; WP_003404794.1; NZ_NVQJ01000001.1.
DR AlphaFoldDB; P9WG09; -.
DR SMR; P9WG09; -.
DR STRING; 83332.Rv0936; -.
DR PaxDb; P9WG09; -.
DR DNASU; 885756; -.
DR GeneID; 885756; -.
DR KEGG; mtu:Rv0936; -.
DR TubercuList; Rv0936; -.
DR eggNOG; COG0581; Bacteria.
DR OMA; YSNWNPF; -.
DR PhylomeDB; P9WG09; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR005672; Phosphate_PstA.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR00974; 3a0107s02c; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphate transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..301
FT /note="Phosphate transport system permease protein PstA 2"
FT /id="PRO_0000060203"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 83..288
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 301 AA; 32236 MW; 1B602BBD39733C40 CRC64;
MGESAESGSR QLPAMSPPRR SVAYRRKIVD ALWWAACVCC LAVVITPTLW MLIGVVSRAV
PVFHWSVLVQ DSQGNGGGLR NAIIGTAVLA IGVILVGGTV SVLTGIYLSE FATGKTRSIL
RGAYEVLSGI PSIVLGYVGY LALVVYFDWG FSLAAGVLVL SVMSIPYIAK ATESALAQVP
TSYREAAEAL GLPAGWALRK IVLKTAMPGI VTGMLVALAL AIGETAPLLY TAGWSNSPPT
GQLTDSPVGY LTYPIWTFYN QPSKSAQDLS YDAALLLIVF LLLLIFIGRL INWLSRRRWD
V
