ID D5VDM6_CAUST Unreviewed; 910 AA.
AC D5VDM6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cseg_0045 {ECO:0000313|EMBL:ADG08576.1};
OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 /
OS LMG 17158 / TK0059) (Mycoplana segnis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG08576.1, ECO:0000313|Proteomes:UP000002629};
RN [1] {ECO:0000313|Proteomes:UP000002629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 /
RC TK0059 {ECO:0000313|Proteomes:UP000002629};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP002008; ADG08576.1; -; Genomic_DNA.
DR RefSeq; WP_013077251.1; NC_014100.1.
DR AlphaFoldDB; D5VDM6; -.
DR STRING; 509190.Cseg_0045; -.
DR KEGG; cse:Cseg_0045; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_18_5; -.
DR Proteomes; UP000002629; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 4.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 4.
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; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
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; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 1.
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; 4.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADG08576.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000313|EMBL:ADG08576.1}.
FT DOMAIN 23..93
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 143..214
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 269..338
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 341..393
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 470..522
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 540..759
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 778..895
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 827
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 910 AA; 98769 MW; 7AF93AB4C8CF3AD2 CRC64;
MSEATIKADG VQATTRGSSS FDEAEAARWF FDNASDLFTV VSPEGRFARV NAAWTTLTGW
SADELVGHPT IKFIHPDSHA ELIDSSRRLR ETGSAINEVR VLCKDGRWVW LQGRSRLGPH
GEMIGLMHDI SGEVEARAQL EAARRTHEML AEAAGIGIWS YEPADARIDW TPDAVAALGL
TPAEIATPEL FFARIAPEQR GKVAEAFSRA VQTGEGGSME YRLRGHHGRW LTFRSTYRAE
PRPGGLHALK GISQNITDVA RSRDKAIWSE RRARRLVEDA PFAVGVYDVD LRLRLVSPKF
LEIFKATEAD VIGRSLQELT NGSRRRFVAG VARALSGEIV TRREDRLLDA EGDEHCLRWE
ARPWRDVNGE IVGVITYMDD VTALAAARRE ARINARRLKV ALGAARAGVY EIDHERASFW
GSPEFHRMVG RRVGYEDVRE AIWPMIHPED RKKLYAAAAE WRRLGDQGAH EYDVRLCPSE
GETRWIRVFH EARRDSSGRP RKAFGLVLDI DEHKRAELAL MAAERAAQAA SEAKAQFLAN
MSHEIRTPMN GVLGVLHVLK RELPSGENAD LLGEALAAGQ MLSTLLDDVI DISRIEAGRL
ELNHEAVDPA ELARGVVRLL AGPASEKGLS LDLDIAQNLG WIQTDATRVR QALFNLIGNA
VKFTVKGSVT VRVRRLGAAD AQRLVFDVVD TGVGVPLAAQ ERLFERFQQA DASTTRRFGG
SGLGLAISRN LARMLGGDIT LRSKPGEGST FSLTIAAPPA AAPAGIGSEA DDLLAGLRVL
VVEDNATNQL VARRILEQLG AAVTVADDGA SGVAAARDGG FDLILMDVQM PGMDGLEAAR
RIRALPGEAA RSPIIALTAN VMAHQRAAYR AAGMDGVAAK PISPAALVAE ILRLSNNGSS
GARAAGGALA
//
