ID A0A2P8F9I9_9RHOB Unreviewed; 640 AA.
AC A0A2P8F9I9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CLV88_11177 {ECO:0000313|EMBL:PSL18332.1};
OS Shimia abyssi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1662395 {ECO:0000313|EMBL:PSL18332.1, ECO:0000313|Proteomes:UP000240418};
RN [1] {ECO:0000313|EMBL:PSL18332.1, ECO:0000313|Proteomes:UP000240418}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100673 {ECO:0000313|EMBL:PSL18332.1,
RC ECO:0000313|Proteomes:UP000240418};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:PSL18332.1}.
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DR EMBL; PYGJ01000011; PSL18332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8F9I9; -.
DR Proteomes; UP000240418; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
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; 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 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; 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; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000240418}.
FT DOMAIN 310..516
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 525..638
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 575
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 640 AA; 69897 MW; A91580F56A155AAA CRC64;
MARVSGTTQA MTIAGLNLIK QALSIYDSNL NLVVSNARFR EMFSIPDHLT RPGASFSNTI
RFLVDNGEYG DVPHEEIETF VAERVERALD FEPHYFERQR ADGRWISVEG SPLPEGGWVA
VYTDITSTKR QEALLRGRSE ELSDQLLQHA EELSATNRKL EATVNTLGEV KRQLTESEAR
MRLTAEMMPA HIAHVGPDRL YTYSNRRLSS VIPGRPSNII GSHISDALGD SAFQSIRPYL
DAAFNGEPSV FEFNDHPSAR RIRVAFTPDG NTGDERGVYI LSMDITEETQ TRVALQQTRR
REIAAQMTSG LAHDFSNLLT IILGTQSKLQ KMALPSEAST LIEATLGAAR RGGTLLNRLA
DITAHRAPNL VPVDMQALLT ELETLATPTL EGKASLIIEN GIPDTPILLD PAMLQDSVVN
LLLNARDACG ENGSILLIAE LIQDTWVQLT IRDSGPGFSP TALQRALEPF FTTKGAEGSG
LGLAMVYDMT KLAGGDVKIA NTDTGGQVSL RLPLRKPVCR SKPGLVLLVE DNADLRGLIR
AMLTDMNHSV IEAASVAEAR ALLDQLPEIN LILSDIMLEG DATGVDLIRE LPNDAVPAYL
MTSLPQTNPL YVKGAARAPM LPKPFTAEQL VKFLHPEAQS
//