ID K0CIZ4_ALCDB Unreviewed; 436 AA.
AC K0CIZ4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=phoR {ECO:0000313|EMBL:AFT72613.1};
GN OrderedLocusNames=B5T_04353 {ECO:0000313|EMBL:AFT72613.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT72613.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT72613.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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; CP003466; AFT72613.1; -; Genomic_DNA.
DR RefSeq; WP_014996664.1; NC_018691.1.
DR AlphaFoldDB; K0CIZ4; -.
DR STRING; 930169.B5T_04353; -.
DR KEGG; adi:B5T_04353; -.
DR PATRIC; fig|930169.3.peg.4319; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_6; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000006286; Chromosome.
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.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFT72613.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW Transferase {ECO:0000313|EMBL:AFT72613.1};
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 12..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..147
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 209..426
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 436 AA; 49426 MW; FF16D5DBF87D23F9 CRC64;
MKSSLAKEVN RIIVLIALSL VAALAVQNVW PLVVGLLGYI VWSTRQLFAL YTWLIREEHT
EPPDSVGLWG EFYTRLEHLF QQERRAQENL QGIILRAQQS VNALEDAVVL IDSHGYLEYW
NHAAHRLMGL NEEKDLGQPL TNLIRHPRFT EYLSCGDFRE PLEIPGPVDD NRILQFRITE
FGVGDQLILA RDVTRLHHLE EMRKDFVANV SHELKTPLTV LKGYLETLQD TVPEEQARLR
RALSQMASQS QRMEALVHDL LLLSRLESTN TDNTHQAVTV HGMLKRMRES ALALAPDKHH
QIVLEVPETA RLVADPAELE SAFGNLITNA VKYTPEGGHI LIRWWQDDKG AHFSVSDDGT
GIDPKHIPRL TERFYRPDTS RVTQTGGTGL GLAIVKHVLI RHGARLEIRS ELGKGSVFIC
HFPRERLVSK PTALAQ
//
