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Database: UniProt
Entry: A0A1B1E9U4_VIBNA
LinkDB: A0A1B1E9U4_VIBNA
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ID   A0A1B1E9U4_VIBNA        Unreviewed;       432 AA.
AC   A0A1B1E9U4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BA894_03155 {ECO:0000313|EMBL:ANQ25516.1};
OS   Vibrio natriegens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=691 {ECO:0000313|EMBL:ANQ25516.1, ECO:0000313|Proteomes:UP000092577};
RN   [1] {ECO:0000313|EMBL:ANQ25516.1, ECO:0000313|Proteomes:UP000092577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 16374 {ECO:0000313|EMBL:ANQ25516.1,
RC   ECO:0000313|Proteomes:UP000092577};
RA   Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.;
RT   "Developing Vibrio natriegens as a novel, fast-growing host for
RT   biotechnology.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system PhoR/PhoB
CC       involved in the phosphate regulon genes expression. PhoR may function
CC       as a membrane-associated protein kinase that phosphorylates PhoB in
CC       response to environmental signals. {ECO:0000256|ARBA:ARBA00025207}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP016351; ANQ25516.1; -; Genomic_DNA.
DR   RefSeq; WP_014230906.1; NZ_JAPQMX010000018.1.
DR   AlphaFoldDB; A0A1B1E9U4; -.
DR   STRING; 691.BA893_02920; -.
DR   GeneID; 70913263; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000092577; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR021766; PhoR.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR014310; Sig_transdc_His_kinase_PhoR.
DR   NCBIfam; TIGR02966; phoR_proteo; 1.
DR   PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF11808; PhoR; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ANQ25516.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:ANQ25516.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   TRANSMEM        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          212..429
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   432 AA;  49638 MW;  73A587996C336492 CRC64;
     MVERLTWKKL AWELAFFYTP WVIVGWIFGY MPWLLLAATA LQLVWHLHNQ VRLSSWLWDE
     KRLTPPSGSG NWESLFNGLY RLQQRQRRKR KELTNLIRRF RNGAESLPDA VVVFRAEGNI
     VWCNKLAQHL LGFHWPEDSG QPISNLIRTP DFIKYLNKQD FSDPLEMRSP INVERMLELR
     IVPYTEGEHL MVVRDVSQLK QLEGMRRNFF ANVSHELRTP MTVLQGYLEM TEDPDMIVGP
     MWTKAHGVMT EQLNRMNALV NQLLTLSKIE AAPMHELEDI VNVPAMLEVL EKEAASLSGD
     DHHKLKFDVD ESLRVFGDDD QLRSAISNLV YNAVKYTPPG ANINVRWYQN AQGACLEVED
     SGDGIEPQHL HRLTERFYRV DKARSRDTGG SGLGLAIVKH ALSHHDSHLE IQSEVGVGSK
     FSFVLPGRLV AK
//
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