ID A0A258V0F5_9GAMM Unreviewed; 320 AA. AC A0A258V0F5; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 14-DEC-2022, entry version 18. DE RecName: Full=Phosphate-binding protein {ECO:0000256|RuleBase:RU367119}; GN ORFNames=B7Y29_00660 {ECO:0000313|EMBL:OYZ09422.1}; OS Thiotrichales bacterium 16-46-22. OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales. OX NCBI_TaxID=1970601 {ECO:0000313|EMBL:OYZ09422.1, ECO:0000313|Proteomes:UP000216165}; RN [1] {ECO:0000313|EMBL:OYZ09422.1, ECO:0000313|Proteomes:UP000216165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=16-46-22 {ECO:0000313|EMBL:OYZ09422.1}; RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S., RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.; RT "Lifting the veil on microbial sulfur biogeochemistry in mining RT wastewaters."; RL Submitted (MAR-2017) 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}. 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:OYZ09422.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NCGV01000004; OYZ09422.1; -; Genomic_DNA. DR AlphaFoldDB; A0A258V0F5; -. DR EnsemblBacteria; OYZ09422; OYZ09422; B7Y29_00660. DR Proteomes; UP000216165; Unassembled WGS sequence. 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 InterPro; IPR024370; PBP_domain. DR InterPro; IPR011862; Phos-bd. DR Pfam; PF12849; PBP_like_2; 1. DR TIGRFAMs; TIGR02136; ptsS_2; 1. PE 3: Inferred from homology; KW Periplasm {ECO:0000256|RuleBase:RU367119}; KW Phosphate transport {ECO:0000256|RuleBase:RU367119}; 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..22 FT /evidence="ECO:0000256|RuleBase:RU367119" FT CHAIN 23..320 FT /note="Phosphate-binding protein" FT /evidence="ECO:0000256|RuleBase:RU367119" FT /id="PRO_5027161480" FT DOMAIN 36..294 FT /note="PBP_domain" FT /evidence="ECO:0000259|Pfam:PF12849" SQ SEQUENCE 320 AA; 33515 MW; 6893FD208F5A5B59 CRC64; MKTIMAALMG VAATTLVAPS FAAVDPALPG YQKVSGVSGN LSSVGSDTLA NLATLWAEEF KRAYPNVNIQ IQAAGSSTAP PALTEGTANI GPMSREMKSK EIEAFEAKYG YKPTGIAVAI DALAVYVHKD NPIKGLTMSQ VDAIFSSTRK CGAAADIANW DQLGGSGALA GKEIQLYGRN SVSGTYGYYK EKALCKGDFK TNVNEQPGSA SVVQSVATSV NAIGYSGIGY KTSGVRALPL AKKDGEPFVE ADEQNAISGK YPLARALYVY VNKAPGKPLD PMVKEFMTLV LSKEGQQVVE KDGYVALPAA VAAKELAKLQ //