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Database: UniProt
Entry: A0A2Z6DV95_HYDTE
LinkDB: A0A2Z6DV95_HYDTE
Original site: A0A2Z6DV95_HYDTE 
ID   A0A2Z6DV95_HYDTE        Unreviewed;       337 AA.
AC   A0A2Z6DV95;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Phosphate-binding protein {ECO:0000256|RuleBase:RU367119};
GN   ORFNames=HPTL_0009 {ECO:0000313|EMBL:BBD76279.1};
OS   Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila).
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales;
OC   Hydrogenophilaceae; Hydrogenophilus.
OX   NCBI_TaxID=297 {ECO:0000313|EMBL:BBD76279.1, ECO:0000313|Proteomes:UP000262004};
RN   [1] {ECO:0000313|EMBL:BBD76279.1, ECO:0000313|Proteomes:UP000262004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TH-1 {ECO:0000313|EMBL:BBD76279.1,
RC   ECO:0000313|Proteomes:UP000262004};
RA   Arai H.;
RT   "Complete genome sequence of Hydrogenophilus thermoluteolus TH-1.";
RL   Submitted (APR-2018) 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   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|RuleBase:RU367119}.
CC       Secreted {ECO:0000256|RuleBase:RU367119}.
CC   -!- SIMILARITY: Belongs to the PstS family. {ECO:0000256|ARBA:ARBA00008725,
CC       ECO:0000256|RuleBase:RU367119}.
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DR   EMBL; AP018558; BBD76279.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z6DV95; -.
DR   KEGG; htl:HPTL_0009; -.
DR   OrthoDB; 5289083at2; -.
DR   Proteomes; UP000262004; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0042301; F:phosphate ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007155; P:cell adhesion; 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.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|RuleBase:RU367119};
KW   Phosphate transport {ECO:0000256|RuleBase:RU367119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000262004};
KW   Secreted {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..27
FT                   /evidence="ECO:0000256|RuleBase:RU367119"
FT   CHAIN           28..337
FT                   /note="Phosphate-binding protein"
FT                   /evidence="ECO:0000256|RuleBase:RU367119"
FT                   /id="PRO_5027162982"
FT   DOMAIN          31..281
FT                   /note="PBP"
FT                   /evidence="ECO:0000259|Pfam:PF12849"
SQ   SEQUENCE   337 AA;  36657 MW;  3DC0A249FC035F3D CRC64;
     MKLRNTLSLV ATLAVAGVVT TPAVTFAAEK IVKIDGSSTV YPVTEAVAEE FQTAQRGKVK
     VTVGISGTGG GFKKFCRGET DISNASRPIL DNEMKLCAEN GIQYIELPVA FDALTVVINP
     KNTWAEEMTV AELKKMWSPE AQGVITNWKQ VSPRFPDRPL KLAGAGSDSG TFDYFTEAIV
     GKAKSSRGDY LASEDDNVVV QFVSSDENAL GYFGLAYYLE NQDKLKAVKI KKDENSPAVA
     PSVETVNNGT YQPLSRPIFI YVNAKAAKEK PEVREFVAFY LKHAGKLAKE VGYVNLPDRA
     YELAMKNFQA MKTGTAFGGH AEVGVSVEEL LARETKE
//
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