ID V9XH35_9NOCA Unreviewed; 374 AA.
AC V9XH35;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Phosphate-binding protein {ECO:0000256|PIRNR:PIRNR002756};
GN ORFNames=Y013_20015 {ECO:0000313|EMBL:AHD22756.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD22756.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD22756.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD22756.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000256|ARBA:ARBA00008725,
CC ECO:0000256|PIRNR:PIRNR002756}.
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DR EMBL; CP006996; AHD22756.1; -; Genomic_DNA.
DR RefSeq; WP_006551794.1; NC_023150.1.
DR AlphaFoldDB; V9XH35; -.
DR GeneID; 29938683; -.
DR KEGG; rpy:Y013_20015; -.
DR PATRIC; fig|1435356.3.peg.4034; -.
DR eggNOG; COG0226; Bacteria.
DR HOGENOM; CLU_034528_0_0_11; -.
DR Proteomes; UP000018781; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0042301; F:phosphate ion binding; IEA:InterPro.
DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro.
DR CDD; cd13565; PBP2_PstS; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR005673; ABC_phos-bd_PstS.
DR InterPro; IPR024370; PBP_domain.
DR NCBIfam; TIGR00975; 3a0107s03; 1.
DR PANTHER; PTHR42996; PHOSPHATE-BINDING PROTEIN PSTS; 1.
DR PANTHER; PTHR42996:SF1; PHOSPHATE-BINDING PROTEIN PSTS; 1.
DR Pfam; PF12849; PBP_like_2; 1.
DR PIRSF; PIRSF002756; PstS; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592,
KW ECO:0000256|PIRNR:PIRNR002756};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|PIRNR:PIRNR002756}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..374
FT /note="Phosphate-binding protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039662537"
FT DOMAIN 47..339
FT /note="PBP"
FT /evidence="ECO:0000259|Pfam:PF12849"
FT BINDING 54..56
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR002756-1"
FT BINDING 88
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR002756-1"
FT BINDING 106
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR002756-1"
FT BINDING 194..196
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR002756-1"
SQ SEQUENCE 374 AA; 37701 MW; 4C12185F57D7A88F CRC64;
MNLKRNGALL GVVAAGALTL AACGTDNNAG SVDVDASASA AACDGKSNLS GAGSSAQKNA
MDQFVSTYIA VCSEKGTNVN VAYNPTGSGD GRTQFIANQI DFAGSDSAIK DEQAAQAAER
CAGNPAWNLP LVFGPVALAY NVEGVDELVL NAETAAKIFN GSITTWNDPA IAALNEGAEL
PDANITPIVR SDSSGTTDNF QQYLETASNG AWTSGAGSDF TGGVGEGAKG SAGVAQAVSG
SPNSITYVEK SFADQNGLSI AQIDNGSGPV ELTEETAGKA IEGAEFVPAS EGDLTLDLSS
IFGSSEEGAY PLVLATYEIV CSAGYDADTA AAVKSFLISA ANEGQEGLSE QGYVPLPDAF
KTRLTESIDA IAAG
//
