ID A0A1Y4A9X7_9BACE Unreviewed; 397 AA.
AC A0A1Y4A9X7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phosphate transport system permease protein {ECO:0000256|RuleBase:RU363054};
GN ORFNames=B5F91_08950 {ECO:0000313|EMBL:OUO19113.1};
OS Bacteroides sp. An322.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1965632 {ECO:0000313|EMBL:OUO19113.1, ECO:0000313|Proteomes:UP000195527};
RN [1] {ECO:0000313|Proteomes:UP000195527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An322 {ECO:0000313|Proteomes:UP000195527};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU363054}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000256|ARBA:ARBA00007069,
CC ECO:0000256|RuleBase:RU363054}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUO19113.1}.
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DR EMBL; NFIN01000014; OUO19113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4A9X7; -.
DR OrthoDB; 9785113at2; -.
DR Proteomes; UP000195527; Unassembled WGS sequence.
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; MetI-like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR024370; PBP_domain.
DR InterPro; IPR011864; Phosphate_PstC.
DR NCBIfam; TIGR02138; phosphate_pstC; 1.
DR PANTHER; PTHR30425; PHOSPHATE TRANSPORT SYSTEM PERMEASE PROTEIN PST; 1.
DR PANTHER; PTHR30425:SF1; PHOSPHATE TRANSPORT SYSTEM PERMEASE PROTEIN PSTC; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF12849; PBP_like_2; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU363054};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592,
KW ECO:0000256|RuleBase:RU363054};
KW Reference proteome {ECO:0000313|Proteomes:UP000195527};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 295..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 368..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 175..386
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 397 AA; 43350 MW; 7490A7034D439FB6 CRC64;
MKRLIDNIAR YILTVSGFTT SVVILLIIGF LFKEAVGLFN NPIVEDGYVL ALNKENDVKK
LSAQQIKNIF DEEITNWKEV GGKDMPITVF RLEDLDKHYT EEELGAEYEF AGAKIAEQIY
QTPGIVAYVP DVLIEGQKNI RYIEDQNIPA KDVLLGNEWF PTATPSPIFG ILPLISGTLW
VSFFAILIAL PFGLAISIYL AEVANEKTRK FLKPIIELLN GIPSVVYGFF GLAVIVPFLQ
QTFNLPVGES GLAGSLVLAI MALPTIITVA EDAMRSCPRN MREASLALGA TQWQTIYKVV
IPFSISGITS GIVLGIGRAI GETMAVLMVT GNAAVMPHSI LEPLRTIPAT IAAELGEAPA
GGAHYQSLFL LGVILFFITL IINSCVEIVS SRNKFKK
//
