ID A0A0L7TEZ6_9GAMM Unreviewed; 437 AA.
AC A0A0L7TEZ6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:KOC93934.1};
GN ORFNames=NG42_11700 {ECO:0000313|EMBL:KOC89512.1}, NG43_08245
GN {ECO:0000313|EMBL:KOC93934.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC93934.1, ECO:0000313|Proteomes:UP000036851};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC89512.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC93934.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC93934.1}.
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; JRXE01000015; KOC89512.1; -; Genomic_DNA.
DR EMBL; JRXF01000010; KOC93934.1; -; Genomic_DNA.
DR RefSeq; WP_052899538.1; NZ_JRXF01000010.1.
DR AlphaFoldDB; A0A0L7TEZ6; -.
DR STRING; 1560201.NG42_11700; -.
DR PATRIC; fig|1560201.3.peg.2486; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; Unassembled WGS sequence.
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 NCBIfam; TIGR00229; sensory_box; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037088};
KW Transferase {ECO:0000313|EMBL:KOC93934.1};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..172
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 210..425
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 437 AA; 50274 MW; 238BF0EDB7D6E502 CRC64;
MLERLSWKRL LLELLLACVP ALILGLLVGY LPWWLLLSVL GVLGWHFYNL LLLSHWLWVD
RTMTPPSGQA SWEPLFYGLY QMQLRNRRRR RELGNLIKRF RSGAESLPDA VVLTTEEGNI
FWCNGLAQQH LGLRWPEDNG QNILNLLRYP EFSRYLRQRD FARPLTLILN NHRHLEFRVM
PYSEGQWLLV ARDVTQMHQL EGARRNFFAN VSHELRTPLT VLQGYLEMMN DAVLEGPARS
KALHTMQEQT RRMDSLVKQL LTLSRIEAAP AIDLQEKVDV PMMLRLLQRE AETLSNGRHE
IHFHTDPHLR VFGNDEQLRS ALSNLVYNSV NHTPAGTRID ISWLRNKSGA HFAVKDNGPG
IAKEHIPRLT ERFYRVDKAR SRATGGSGLG LAIVKHALSH HNSRLDITSV ADVETCFAFT
LAPRLIVPAE LPENAKR
//
