ID A0A345P839_9GAMM Unreviewed; 435 AA.
AC A0A345P839;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:AXI03448.1};
GN ORFNames=HYN46_11720 {ECO:0000313|EMBL:AXI03448.1};
OS Aquirhabdus parva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Aquirhabdus.
OX NCBI_TaxID=2283318 {ECO:0000313|EMBL:AXI03448.1, ECO:0000313|Proteomes:UP000253940};
RN [1] {ECO:0000313|EMBL:AXI03448.1, ECO:0000313|Proteomes:UP000253940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0046 {ECO:0000313|EMBL:AXI03448.1,
RC ECO:0000313|Proteomes:UP000253940};
RA Kim M., Yi H.;
RT "Genome sequencing of Moraxellaceae gen. HYN0046.";
RL Submitted (JUL-2018) 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; CP031222; AXI03448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345P839; -.
DR KEGG; mbah:HYN46_11720; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000253940; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 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 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:AXI03448.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000253940};
KW Transferase {ECO:0000313|EMBL:AXI03448.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022592}.
FT TRANSMEM 20..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..432
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 435 AA; 50517 MW; 75F35D0FD9B4F551 CRC64;
MSNSTTSLLD FVYQDLLRLI GLVLIFFCIG WVVGMPWLAV LLALFLFLLL QWYSLYRLYR
WMQHTPDQEP PELGGVWSAL LYNITRIQIS EHRSRKNLLG VISRAQTSVA ALEEAVVLID
ASSLIEWWNP AAEKILGLKS GDQGRNILNF CRAPEFVSYY QQGNYSQEIK LKSWINEERY
FQCKLTRFGQ NDRLLVAYDV TRLHNLELMR KDFVDNVSHE LRTPLTVLSG YLETYMDQDD
LNPRWRRGFE QMRQQTTRMT NIVKDLLLLS RLENSSAQTE RKVIDMPYLL NKIFDDAQAY
NAEFKHELNL EIESFRSILG AEQELTSAFT NLITNAIKYT PKGGIIRVRW FDDGDDCCFS
VTDNGIGIES HHINRLTERF YRVDSDRSRD TGGTGLGLAI VKHVMLQHEG RLEISSKREQ
GSTFLCRFPK ERLVE
//
