ID A4C752_9GAMM Unreviewed; 442 AA.
AC A4C752;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 13-SEP-2023, entry version 90.
DE RecName: Full=Phosphate regulon sensor protein PhoR {ECO:0000256|ARBA:ARBA00019665};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PTD2_13339 {ECO:0000313|EMBL:EAR29806.1};
OS Pseudoalteromonas tunicata D2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=87626 {ECO:0000313|EMBL:EAR29806.1, ECO:0000313|Proteomes:UP000006201};
RN [1] {ECO:0000313|EMBL:EAR29806.1, ECO:0000313|Proteomes:UP000006201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D2 {ECO:0000313|EMBL:EAR29806.1,
RC ECO:0000313|Proteomes:UP000006201};
RA Moran M.A., Kjelleberg S., Egan S., Saunders N., Thomas T., Ferriera S.,
RA Johnson J., Kravitz S., Halpern A., Remington K., Beeson K., Tran B.,
RA Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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};
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:EAR29806.1}.
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DR EMBL; AAOH01000002; EAR29806.1; -; Genomic_DNA.
DR RefSeq; WP_009837680.1; NZ_AAOH01000002.1.
DR AlphaFoldDB; A4C752; -.
DR STRING; 87626.PTD2_13339; -.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_89_2_6; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000006201; 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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Phosphate transport {ECO:0000256|ARBA:ARBA00022592};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW 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 442 AA; 50941 MW; B96B52195163761D CRC64;
MYRVINKRTL TKRLVIYFLP LLLIGVLIGA PFLLLFLGAS VLMFWHYRQL YRLSDWLINQ
RSFNPPEGDG TWEQIFEGIY RLQHRNRNKR NELAELIRRF REGAEAVPDA VIVLQRDFSI
VWCNQLALKV LGLKWPMDHG QRLDNLIRHP KFSLYMQAKK FEEPLELISP LGIEQVLEFR
VMPYADAQLM MVVRDVTRLK QLEQMRKDFV ANVSHELRTP LTVIAGYLEM MEPDDLPPAR
VWGKAHGTML EQCKRMDSLV SQLLSLSRIE GLRRIDQDKT VDVPKMLKLV MIEAETLNRD
KHHTLHCEIE EGLFILGGED ELRSAFSNLV FNAVHYTPAE GEITVKWHVN NGCAQFSVTD
NGDGIAPEHI HRLTERFYRV DKARSRKTGG SGLGLAITKH VLSRHESELL IKSEVGKGSC
FSFSFASNRV KQQVTDALLQ LD
//
