ID Q2RL86_MOOTA Unreviewed; 309 AA.
AC Q2RL86;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Phosphate-binding protein {ECO:0000256|RuleBase:RU367119};
GN OrderedLocusNames=Moth_0473 {ECO:0000313|EMBL:ABC18803.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX NCBI_TaxID=264732 {ECO:0000313|EMBL:ABC18803.1};
RN [1] {ECO:0000313|EMBL:ABC18803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 39073 {ECO:0000313|EMBL:ABC18803.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Saunders E.H., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Anderson I., Richardson P., Ragsdale S.;
RT "Complete sequence of Moorella thermoacetica ATCC 39073.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the system for phosphate transport across the
CC cytoplasmic membrane. {ECO:0000256|RuleBase:RU367119}.
CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in
CC phosphate import. {ECO:0000256|ARBA:ARBA00002841}.
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:0000256|ARBA:ARBA00011529, ECO:0000256|RuleBase:RU367119}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193,
CC ECO:0000256|RuleBase:RU367119}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004193, ECO:0000256|RuleBase:RU367119}.
CC Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000256|ARBA:ARBA00008725,
CC ECO:0000256|RuleBase:RU367119}.
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DR EMBL; CP000232; ABC18803.1; -; Genomic_DNA.
DR RefSeq; YP_429346.1; NC_007644.1.
DR AlphaFoldDB; Q2RL86; -.
DR STRING; 264732.Moth_0473; -.
DR EnsemblBacteria; ABC18803; ABC18803; Moth_0473.
DR KEGG; mta:Moth_0473; -.
DR PATRIC; fig|264732.11.peg.510; -.
DR eggNOG; COG0226; Bacteria.
DR HOGENOM; CLU_026228_5_0_9; -.
DR OrthoDB; 9790048at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042301; F:phosphate ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-UniRule.
DR CDD; cd13653; PBP2_phosphate_like_1; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR024370; PBP_domain.
DR InterPro; IPR011862; Phos-bd.
DR NCBIfam; TIGR02136; ptsS_2; 1.
DR PANTHER; PTHR30570; PERIPLASMIC PHOSPHATE BINDING COMPONENT OF PHOSPHATE ABC TRANSPORTER; 1.
DR PANTHER; PTHR30570:SF4; PHOSPHATE-BINDING PROTEIN PSTS; 1.
DR Pfam; PF12849; PBP_like_2; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU367119};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU367119};
KW Membrane {ECO:0000256|RuleBase:RU367119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU367119};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592,
KW ECO:0000256|RuleBase:RU367119}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367119}.
FT DOMAIN 41..278
FT /note="PBP"
FT /evidence="ECO:0000259|Pfam:PF12849"
FT REGION 30..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 32839 MW; 1CCE322862A937F9 CRC64;
MLSKGKWLAI LVIALVAVLA VAGCGKKEFP APQQGSSQQN SNQQSGGSGA ITAAGSTALQ
PLVDEAAKQY MEKNPGVRIV VNGGGSGNGL SQVFQGAVQI GNSDIFAEEK DGIDASQLVD
HKVAVVGMAA VVNPDVKVDN LTQQQLIDIF TGKITNWKDV GGPDQKINIV NRPKGSGTRA
TFKKYALNGA EEAQGIAMEQ DASGTVRKTI AETPGAIGYL ALSYIDSSVR PLKIDGVEPT
AANIVDNKYK VWAYEHMYTK GQPTGEVKKF LDFIMSDEVQ KNLVTKMGYI PVTDMKVERD
AQGNVTPKK
//
