ID D7A028_STAND Unreviewed; 746 AA.
AC D7A028;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Snov_1990 {ECO:0000313|EMBL:ADH89289.1};
OS Starkeya novella (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM
OS 12100 / NBRC 12443 / NCIMB 10456).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Ancylobacter.
OX NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH89289.1, ECO:0000313|Proteomes:UP000006633};
RN [1] {ECO:0000313|EMBL:ADH89289.1, ECO:0000313|Proteomes:UP000006633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC
RC 12443 / NCIMB 10456 {ECO:0000313|Proteomes:UP000006633};
RX PubMed=23450099; DOI=10.4056/sigs.3006378;
RA Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A., Copeland A.,
RA Berry K.W., Glavina Del Rio T., Hammon N., Dalin E., Tice H., Pitluck S.,
RA Richardson P., Bruce D., Goodwin L.A., Han C., Tapia R., Detter J.C.,
RA Chang Y.J., Jeffries C.D., Land M., Hauser L., Kyrpides N.C., Goker M.,
RA Ivanova N., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the facultatively chemolithoautotrophic and
RT methylotrophic alpha Proteobacterium Starkeya novella type strain (ATCC
RT 8093(T)).";
RL Stand. Genomic Sci. 7:44-58(2012).
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; CP002026; ADH89289.1; -; Genomic_DNA.
DR RefSeq; WP_013166793.1; NC_014217.1.
DR AlphaFoldDB; D7A028; -.
DR STRING; 639283.Snov_1990; -.
DR KEGG; sno:Snov_1990; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_2_1_5; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000006633; Chromosome.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ADH89289.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:ADH89289.1}.
FT DOMAIN 6..115
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 204..471
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 629..745
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 114..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..160
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 678
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 746 AA; 80679 MW; FF271DFD65F8F641 CRC64;
MSTTSKDELR IRLLAIFREE AADHLRAIAR EVSGLERETR PAQVDERLEQ LFRTVHTLKG
AARSLSIGSI ERLCHEIEDL CSEGRQAGAF DPEARTLLRE LTDELVHVTR QALAGPAAAP
PAPAPEKSAE PPSPPAPPPM PIAPEPPAAA TPPPPAAKSG RKPGARPEPR PDPRPLELVA
PAMEMAGGPG FVRLETSRLQ RLGLMAEELI GPRLAMQARV DEARDLVGRL AALHADEGPS
ERHPKELRAA EQSARQFLAS LAEDNRTLRG VIDGLVEELR RTRMMPASEM LAVFPAMVAD
LAGEVGKEVV WRTLGADLLI DRQIAERIKD PLIHIVRNAV DHGIEPAEAR AAAGKPAQGA
VSLNLEPAEG GRVAIEVADD GAGIDLPGLR EAAVRNRFVS REEASRLSDE ALAEMVFESS
LSTRTVISPV SGRGLGLAIV RERVERLGGS VHIASTPGKG TVLRLEVPAA LANFHGIGAR
AGDAFVIWPR EAVERSLALP EDAYEVALAR GAVQIDDVLL PFGSLAHVLG QPPEAAPAGR
RGLRSCLVIR YKERRGVLAV DEVTGNCEVV VKELRPPLLR VRHVLAAGLL GNGRLGLILR
TADVLDTLIN HPRRAAPAPR PVRRQGKPRL LVVDDSITTR AMETGLLEAA GYEVHAASDG
MEAWTVLQSG EFDAIISDID MPRMDGFELT ERIRADARLK RLPIVLVTAL EKREDHERGL
RLGANAYMMK SAFDQSMLID LVRRVL
//
