ID A0A1I1T753_9BACI Unreviewed; 336 AA.
AC A0A1I1T753;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Phosphate-binding protein {ECO:0000256|RuleBase:RU367119};
GN ORFNames=SAMN05216238_102146 {ECO:0000313|EMBL:SFD54464.1};
OS Lentibacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=640948 {ECO:0000313|EMBL:SFD54464.1, ECO:0000313|Proteomes:UP000199474};
RN [1] {ECO:0000313|EMBL:SFD54464.1, ECO:0000313|Proteomes:UP000199474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22530 {ECO:0000313|EMBL:SFD54464.1,
RC ECO:0000313|Proteomes:UP000199474};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOMR01000002; SFD54464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1T753; -.
DR STRING; 640948.SAMN05216238_102146; -.
DR OrthoDB; 9790048at2; -.
DR Proteomes; UP000199474; Unassembled WGS sequence.
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; cd13654; PBP2_phosphate_like_2; 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:SF1; 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};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367119};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367119}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU367119"
FT CHAIN 21..336
FT /note="Phosphate-binding protein"
FT /evidence="ECO:0000256|RuleBase:RU367119"
FT /id="PRO_5039745734"
FT DOMAIN 50..303
FT /note="PBP"
FT /evidence="ECO:0000259|Pfam:PF12849"
FT REGION 26..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 36412 MW; 171CEF08F8D61918 CRC64;
MKSKSLWLLA VISLLLVVLA ACGNAEGSED GGDEEANSNT EENTSAEGSS ESEGEMTEVV
VDGSSTVFPV MEAVAEEYQK ENPDARVNIG TSGSGGGFEK FAAGETHISN ASRPIKDEEK
QALEETGIEY TEFEIALDGL SIVVNTENDW VDQLTVEELN KMWSADGDVT TWADVREGWP
EEEIEFYSPG ADSGTFDYFS EVVFGEEGDI RQDASLSEDD NVLVQGVTGS KNAIGYFGYA
YYAENDDQLK AVPIVNDSGE AVKPDQETVQ SGEYNPFARP LFVYVKHSTL EDESVYNFAK
YALENAGAMA ESVGYVAKPD SAYEEALNKL DEIAGK
//
