ID B3PF44_CELJU Unreviewed; 761 AA.
AC B3PF44;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=CJA_3358 {ECO:0000313|EMBL:ACE84940.1};
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84940.1, ECO:0000313|Proteomes:UP000001036};
RN [1] {ECO:0000313|EMBL:ACE84940.1, ECO:0000313|Proteomes:UP000001036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84940.1,
RC ECO:0000313|Proteomes:UP000001036};
RX PubMed=18556790; DOI=10.1128/JB.01701-07;
RA Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE84940.1; -; Genomic_DNA.
DR AlphaFoldDB; B3PF44; -.
DR STRING; 498211.CJA_3358; -.
DR KEGG; cja:CJA_3358; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_393164_0_0_6; -.
DR Proteomes; UP000001036; 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; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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; 3.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001036}.
FT DOMAIN 139..212
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 216..269
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 270..345
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 348..400
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 475..526
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 530..749
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 119..146
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 761 AA; 86316 MW; 8D3D8B2D2CF91E11 CRC64;
MVCEAPIAVI SLIDAQRQWF KSCIGLGGEE TERDLAFCAH AILQPDTLME VRDAHLDPRF
ADHPFVLGEP RLRFYAGMPL EITPGIALGT LCIIDYVPRQ LTPHQRQALM LLANQVVQLL
QLHESNQRVK QQSIQLERER KNLDLVIRGA NMGTWQWNVQ TGEVILNERW ASILGFTLAE
LSPMSIQAWE HMIHPDDLPA ARQSLEQHFA EEMDFYDSKF RMCHKDGTWV WVYTRGRVLS
RTDQGEPLWM FGTHADITEL QVYQERLQAS EERLQSMIRN FPGAVYRCEN NPLWTMHYIS
PAIERLSGYL PESFMGDGAI SLTQITHPED IARHYYRVQM AVNRREPFDV VYRLLHRDGS
WRYVQEVGTG IYDEQGQLQF LDGFIWDITQ AEEARNAIQL NEQKLSSLYQ LSPVAIALHR
LADGAFVEGN PEFYRMLGYT AEEFPGLSYW DITPTEYAAA EMEQLESLHI TGRYGPYEKH
YLHKDGHQIP VLLNGVLIEN SHREKQIWSI IQDITERKRI EQMKNEFVSA VSHELRTPLT
SISGSLGLIL NGMLGEVPVR ARDMLVIAHK NALRLAHLIN DLLDMEKLAA GKLDFYMQPQ
AVLPIVEQSI ESMRGYAENY GVSLVFDAVA GDASVNIDAQ RLQQVLTNFL SNAVKFSPEG
SRVILRMRVQ GRELCLAVTD QGPGISDEFR TRIFQKFSQA DASSSRQRGG TGLGLAISKE
LVERMGGNIG FDSIPGEGAT FYACFPLLTD GRMQSTVGEG S
//
