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Database: UniProt
Entry: A4A3L9_9GAMM
LinkDB: A4A3L9_9GAMM
Original site: A4A3L9_9GAMM 
ID   A4A3L9_9GAMM            Unreviewed;       424 AA.
AC   A4A3L9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=KT71_16521 {ECO:0000313|EMBL:EAQ99292.1};
OS   Congregibacter litoralis KT71.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Congregibacter.
OX   NCBI_TaxID=314285 {ECO:0000313|EMBL:EAQ99292.1, ECO:0000313|Proteomes:UP000019205};
RN   [1] {ECO:0000313|EMBL:EAQ99292.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ99292.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=17299055; DOI=10.1073/pnas.0608046104;
RA   Fuchs B.M., Spring S., Teeling H., Quast C., Wulf J., Schattenhofer M.,
RA   Yan S., Ferriera S., Johnson J., Glockner F.O., Amann R.;
RT   "Characterization of a marine gammaproteobacterium capable of aerobic
RT   anoxygenic photosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2891-2896(2007).
RN   [2] {ECO:0000313|EMBL:EAQ99292.1, ECO:0000313|Proteomes:UP000019205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT71 {ECO:0000313|EMBL:EAQ99292.1,
RC   ECO:0000313|Proteomes:UP000019205};
RX   PubMed=19287491; DOI=10.1371/journal.pone.0004866;
RA   Spring S., Lunsdorf H., Fuchs B.M., Tindall B.J.;
RT   "The photosynthetic apparatus and its regulation in the aerobic
RT   gammaproteobacterium Congregibacter litoralis gen. nov., sp. nov.";
RL   PLoS ONE 4:E4866-E4866(2009).
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};
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:EAQ99292.1}.
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DR   EMBL; AAOA02000001; EAQ99292.1; -; Genomic_DNA.
DR   RefSeq; WP_008295737.1; NZ_CM002299.1.
DR   AlphaFoldDB; A4A3L9; -.
DR   STRING; 314285.KT71_16521; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_89_2_6; -.
DR   OrthoDB; 9813151at2; -.
DR   Proteomes; UP000019205; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
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   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; 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; 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:EAQ99292.1};
KW   Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019205};
KW   Transferase {ECO:0000313|EMBL:EAQ99292.1};
KW   Transport {ECO:0000256|ARBA:ARBA00022592}.
FT   DOMAIN          211..424
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   424 AA;  48226 MW;  B8B2C7145C7048B0 CRC64;
     MSLAGSWRAE LRKLLLVLAA SGVLGWVTGY TLEMLCIGLS VLSGIWLWQL WLMRRWLQDP
     DQPPPESGGI WGLVYDTIYG LQRENREARG RLQSTVDYLR SSFASMRDGV LILTQSGAIE
     WSNDAAEGLL GLQYPRDRGQ PVLNLLRWPA FHDYFLNGDF QQPLQIPNDR NSRQILQVEI
     TTFAGGDFLL FFRDVTRVVQ MEQMRRDFVG NVSHELRTPL TVFKGYLDTL VSSELFEDPR
     FQKAAAQMDM QVQRMENLLT DLLWLSRIET VSEDRETEDV NMVAMLEELR EELRSSHPDR
     LVVLEVETQD TVKGNYRELR SAVSNLVINA LKYSEDDKPV RVSWVHGNGA LVLNVVDAGV
     GIEEEHIARI TERFYRVDES RNARTGGTGL GLAIVKHVAA SHRAELIIES EPGRGSRFAL
     HFPL
//
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