ID B4CVM1_9BACT Unreviewed; 891 AA.
AC B4CVM1;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CfE428DRAFT_0708 {ECO:0000313|EMBL:EDY21463.1};
OS Chthoniobacter flavus Ellin428.
OC Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC Chthoniobacteraceae; Chthoniobacter.
OX NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY21463.1, ECO:0000313|Proteomes:UP000005824};
RN [1] {ECO:0000313|EMBL:EDY21463.1, ECO:0000313|Proteomes:UP000005824}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ellin428 {ECO:0000313|EMBL:EDY21463.1,
RC ECO:0000313|Proteomes:UP000005824};
RX PubMed=21460085; DOI=10.1128/JB.00295-11;
RA Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA Smidt H.;
RT "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT heterotrophic soil bacterium.";
RL J. Bacteriol. 193:2902-2903(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 -!- 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:EDY21463.1}.
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DR EMBL; ABVL01000002; EDY21463.1; -; Genomic_DNA.
DR AlphaFoldDB; B4CVM1; -.
DR STRING; 497964.CfE428DRAFT_0708; -.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR InParanoid; B4CVM1; -.
DR Proteomes; UP000005824; Unassembled WGS sequence.
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; 3.
DR CDD; cd00156; REC; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; IPR013656; PAS_4.
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; PF00989; PAS; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
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; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
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; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EDY21463.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005824};
KW Transferase {ECO:0000313|EMBL:EDY21463.1}.
FT DOMAIN 9..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 150..206
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 224..274
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 271..313
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 392..456
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 463..515
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 528..750
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 771..887
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 60
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 822
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 891 AA; 98661 MW; C5B3A46AE89D528B CRC64;
MNRRAQPLYA LLVEDSEDDA LLLVEALSRG GFAPDWKRVV DEEGMRAALR SREWEIVFCD
YNLPNFNAPS AIRVLRECGC DAPIIIVSGA VGEDVAVESL RQGANDYLPK NNLRRLVPAV
ERELRESEAR RGQQLSEAKK HFAEEALRAS EERYRVLFER NPVPMWVYDC TTWRFLQVNE
AAIAHYGYSR EEFMALSVLD LRPGEDAILL GESRSNHRND DPLTRGTWRH RKKDGTIFFV
EVVTQPIKYG TTKARIAQAL DITERKVAEK ELTRIKMAVD FSTDAIAILD DASISVYHNR
AFEELLGYTP EELNAVEGGP RALFVHQQVV DEIFSSVAQS GSWAGDAYLA SKSNKPIQLF
VRVNAALDGA GRIITTSIVC TDLREQKRAQ GKIEEQAALL DHAQDAIIVH DLAGRIKYWN
KSARRVFGWT PAEVTGRRVQ DILYSTPEPF DEAMVELLRT GSWTGDLKQQ NRDDKEVLIE
GRWTLVRDEF GDPKSVLSIN TDITAKKKLE SQFLRAQRME SIGTLAGGIA HDLNNVLGPI
IMAVDLFRLK MTDPQDLELL ETVSVSARRG ADMVKQVLSF ARGLEGQRTL VRPVQLLKEV
QRIARDTFPK FISVDITTAE DTWSLLGDPT QLHQVLLNLC VNARDAMPQG GRLTLNACNQ
RIDDHFAAMH PEARPGPHVV LEVADSGTGM TPDVIEKIFE PFFTTKEVGK GTGLGLSTTL
AIVRSHNGFV TVESHPGKGT KFRVHLPAEL DDVEANHSEG GDVFPRGQGE CILVIDDEAS
VRSITSQTLE AFGYRVVIAV DGAEGVAKYA QHMNEIAAVI TDMMMPVMDG VATIRALSRL
DPNIKIIAAS GLATKGAEAE AAGAGVKLFL PKPYTASSLL VALRDLLRPG N
//
