ID F2IWG1_POLGS Unreviewed; 652 AA.
AC F2IWG1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=SL003B_0830 {ECO:0000313|EMBL:ADZ69260.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ69260.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ69260.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
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; CP002568; ADZ69260.1; -; Genomic_DNA.
DR RefSeq; WP_013651577.1; NC_015259.1.
DR AlphaFoldDB; F2IWG1; -.
DR STRING; 991905.SL003B_0830; -.
DR KEGG; pgv:SL003B_0830; -.
DR PATRIC; fig|991905.3.peg.843; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_5; -.
DR OrthoDB; 9796100at2; -.
DR Proteomes; UP000008130; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008130}.
FT DOMAIN 220..272
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 285..509
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 534..650
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 584
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 652 AA; 71255 MW; B73AAEEE9E3F1CF7 CRC64;
MTRSDPQSEL LDLLQAALDH VNQGFSVFDA DLRLVAWNRG LWEMLDFPQA LAKRGTHLAD
FLRVNAERGE YGPGDTEAKI ARRVERARLF QPHYFERIRP NGQVIAVSGR PLPQGGFVTT
YTDVTEERRR QEKLERTVEE RTRALRQSED WLRLVTDNVP ALIAYMGPGP VFRFANRRYA
DWFGHSIASI VGRSPQDVVG QELYAELEPH IEHAFAGNAV SYEYSRRKAD GDVAYMRSTL
IPDMTIDGRT LGVFVLSLDA TEQKRSEATL VQSQRMDAVG KLTGGLAHDF NNLLAILMGN
LLSLKRKGQD VTVQEVLAHL EPMLQAAQRG TDLTQRLLAF SRGKATETHD VPLQGVLNNV
ATLLKGSMPG NVALEIRSST DRLIARLDPT QIENAIVNLV FNARDALPDG GKITITLDET
DLPVKEAAKA GLGPGLYARL TVRDTGIGMS EDTRLRVFEP FFTTKQFGTG SGLGLSMVYG
FARQSGGSVD IETVPGEGTA VTLLLPARRR PDTIRAAGPW PDDLPPLPEG NGELILLVED
DAAVAATITE QLQDLGYTVL AAESAEDARS LARDVPEIRA LLTDIVMPGQ VNGLALARAI
STERASLGIA LMTGYADWSG LGADGSEPPF PVLAKPFDSR TLAETLRTIL TT
//
