PSTC1_MYCTU
ID PSTC1_MYCTU Reviewed; 338 AA.
AC P9WG07; L0T7Y5; O05867; P0A628; P95303;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Phosphate transport system permease protein PstC 1;
GN Name=pstC1; Synonyms=pstC; OrderedLocusNames=Rv0935; ORFNames=MTCY08D9.04c;
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).
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: 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; Z47982; CAA88025.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP43683.1; -; Genomic_DNA.
DR PIR; G70584; G70584.
DR RefSeq; WP_003404792.1; NZ_NVQJ01000001.1.
DR RefSeq; YP_177771.1; NC_000962.3.
DR AlphaFoldDB; P9WG07; -.
DR STRING; 83332.Rv0935; -.
DR PaxDb; P9WG07; -.
DR DNASU; 885644; -.
DR GeneID; 885644; -.
DR KEGG; mtu:Rv0935; -.
DR TubercuList; Rv0935; -.
DR eggNOG; COG0573; Bacteria.
DR OMA; CITLCLN; -.
DR PhylomeDB; P9WG07; -.
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: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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphate transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..338
FT /note="Phosphate transport system permease protein PstC 1"
FT /id="PRO_0000060218"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 87..320
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 319..321
FT /note="AAR -> G (in Ref. 1; CAA88025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 34793 MW; 10D7BA65D72F7F96 CRC64;
MLARAGEVGR AGPAIRWLGG IGAVIPLLAL VLVLVVLVIE AMGAIRLNGL HFFTATEWNP
GNTYGETVVT DGVAHPVGAY YGALPLIVGT LATSAIALII AVPVSVGAAL VIVERLPKRL
AEAVGIVLEL LAGIPSVVVG LWGAMTFGPF IAHHIAPVIA HNAPDVPVLN YLRGDPGNGE
GMLVSGLVLA VMVVPIIATT THDLFRQVPV LPREGAIALG MSNWECVRRV TLPWVSSGIV
GAVVLGLGRA LGETMAVAMV SGAVLGAMPA NIYATMTTIA ATIVSQLDSA MTDSTNFAVK
TLAEVGLVLM VITLLTNVAA RGMVRRVSRT ALPVGRGI
