ID Q485A7_COLP3 Unreviewed; 927 AA.
AC Q485A7;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=CPS_1620 {ECO:0000313|EMBL:AAZ25511.1};
OS Colwellia psychrerythraea (strain 34H / ATCC BAA-681) (Vibrio
OS psychroerythus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=167879 {ECO:0000313|EMBL:AAZ25511.1, ECO:0000313|Proteomes:UP000000547};
RN [1] {ECO:0000313|EMBL:AAZ25511.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34H {ECO:0000313|EMBL:AAZ25511.1};
RX PubMed=16043709; DOI=10.1073/pnas.0504766102;
RA Methe B.A., Nelson K.E., Deming J.W., Momen B., Melamud E., Zhang X.,
RA Moult J., Madupu R., Nelson W.C., Dodson R.J., Brinkac L.M.,
RA Daugherty S.C., Durkin A.S., DeBoy R.T., Kolonay J.F., Sullivan S.A.,
RA Zhou L., Davidsen T.M., Wu M., Huston A.L., Lewis M., Weaver B.,
RA Weidman J.F., Khouri H., Utterback T.R., Feldblyum T.V., Fraser C.M.;
RT "The psychrophilic lifestyle as revealed by the genome sequence of
RT Colwellia psychrerythraea 34H through genomic and proteomic analyses.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10913-10918(2005).
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; CP000083; AAZ25511.1; -; Genomic_DNA.
DR RefSeq; WP_011042452.1; NC_003910.7.
DR AlphaFoldDB; Q485A7; -.
DR STRING; 167879.CPS_1620; -.
DR KEGG; cps:CPS_1620; -.
DR HOGENOM; CLU_315161_0_0_6; -.
DR Proteomes; UP000000547; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 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; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 3.
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; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
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; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AAZ25511.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:AAZ25511.1}.
FT DOMAIN 365..417
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 418..488
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 560..781
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 807..920
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 856
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 927 AA; 103983 MW; B689C4E9D7E2D66A CRC64;
MFKSPENDSL VSAVFDSSPI GIQIIDLETG MREKINQTAC VLLGDTKDNL MAKSVFEDCT
WLGKDKFLFV IERLKENKTL KNHIVQFENH QGNELTISYD ISEFKYRSKR LVTVSMNDVT
EQHYLLKNIS DTANLIFSDD DTSFFDNVTL KIAELFEAAH VFIGLNNFDD GLKMKTVSYC
CYNQIIENFT YNLKHTPCAN IVKDINGNAC YVYQDVQTLF PKDSFFIEKK IKSYIGMPIF
DINKKTIGGL ILLFTKDINK NTYWEDLLKI FSGKISSELK HLTLHNTHYE AQQHLKLYSE
QAPLALFKWD LGFNLLECNQ SAISMLNYTE DELKQCDFIS ALVPINEQKR VNKTCSDLLV
NEGGEHGFNS LIKQNGNIIL TEWHNSLIKD DSGAAIGVIS IVKDITQERQ QLKRLAQKET
EKREIINAII DAVITINSKG IILSVNAATE KMFGYSVDEL LGENIKLLMP KSTAVKHDTY
LENYLQTKEA QIIGIGRKVI AIKKNGQEFP IYLGIAELSP DENNNIRYVG TCHDLSLFTE
QQNKLQRIQK MDALGKLTGG IAHDFNNLLG IVSGFGELLE LKLGQDPKLS KYCRQIITAS
ERGSELTRKL LDFSKQESKK STVCNINDLL TATQGMIAKT LTVLVTVNYT LADDLWCSTI
DISAFDDVIL NLCINAKHAM SNGGLLSIST QNVTLSAIEA ERYNLTAGDF VSLTITDNGC
GMNDKVKRQI FEPFYTTKGD EGTGLGLSQV YGFITSSQGS IYVYSETNMG TSINIYLPRS
KPKESKNVLS KNVLSKSKYI SLKGKENILV VDDEFSLGLL AKTILENEGY TVFQTSSGED
ALFCLTAHNI DLIISDVIMP KTTGYQLIEK VRALDINIPI ILATGFDGYI NISKGNYSDI
PIISKPYTSY ELLTQTRMSL DSKKIEN
//
