PSTC2_MYCTU
ID PSTC2_MYCTU Reviewed; 324 AA.
AC P9WG05; L0T849; O86344; P0A630; Q50797;
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 PstC 2;
GN Name=pstC2; OrderedLocusNames=Rv0929; ORFNames=MTCY21C12.23;
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=8843165; DOI=10.1016/0014-5793(96)00953-2;
RA Braibant M., Lefevre P., de Wit L., Ooms J., Peirs P., Huygen K.,
RA Wattiez R., Content J.;
RT "Identification of a second Mycobacterium tuberculosis gene cluster
RT encoding proteins of an ABC phosphate transporter.";
RL FEBS Lett. 394:206-212(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 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 [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 ABC transporter complex PstSACB involved in
CC phosphate import; probably responsible for the translocation of the
CC substrate 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:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: 5-fold by phosphate starvation, part of the pstS3-pstC2-
CC pstA1 operon. {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; Z47983; CAA88026.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43677.1; -; Genomic_DNA.
DR PIR; A70584; A70584.
DR RefSeq; NP_215444.1; NC_000962.3.
DR RefSeq; WP_003404779.1; NZ_NVQJ01000001.1.
DR AlphaFoldDB; P9WG05; -.
DR STRING; 83332.Rv0929; -.
DR PaxDb; P9WG05; -.
DR DNASU; 885585; -.
DR GeneID; 45424895; -.
DR GeneID; 885585; -.
DR KEGG; mtu:Rv0929; -.
DR TubercuList; Rv0929; -.
DR eggNOG; COG0573; Bacteria.
DR OMA; VIRMSVL; -.
DR PhylomeDB; P9WG05; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
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; IPR011864; Phosphate_PstC.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR02138; phosphate_pstC; 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..324
FT /note="Phosphate transport system permease protein PstC 2"
FT /id="PRO_0000060219"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 85..314
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 19
FT /note="Missing (in Ref. 1; CAA88026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 34262 MW; 0C54657C8A3CEAC5 CRC64;
MVTEPLTKPA LVAVDMRPAR RGERLFKLAA SAAGSTIVIA ILLIAIFLLV RAVPSLRANH
ANFFTSTQFD TSDDEQLAFG VRDLFMVTAL SSITALVLAV PVAVGIAVFL THYAPRRLSR
PFGAMVDLLA AVPSIIFGLW GIFVLAPKLE PIARFLNRNL GWLFLFKQGN VSLAGGGTIF
TAGIVLSVMI LPIVTSISRE VFRQTPLIQI EAALALGATK WEVVRMTVLP YGRSGVVAAS
MLGLGRALGE TVAVLVILRS AARPGTWSLF DGGYTFASKI ASAASEFSEP LPTGAYISAG
FALFVLTFLV NAAARAIAGG KVNG
