ID V4JIE0_9GAMM Unreviewed; 429 AA.
AC V4JIE0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=N838_12080 {ECO:0000313|EMBL:ESQ14309.1};
OS Thiohalocapsa sp. PB-PSB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiohalocapsa.
OX NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ14309.1, ECO:0000313|Proteomes:UP000017935};
RN [1] {ECO:0000313|EMBL:ESQ14309.1, ECO:0000313|Proteomes:UP000017935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA Orphan V.J.;
RT "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT consortia of the Sippewissett salt marsh.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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:ESQ14309.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AVFR01000667; ESQ14309.1; -; Genomic_DNA.
DR AlphaFoldDB; V4JIE0; -.
DR Proteomes; UP000017935; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000017935};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 155..210
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 218..429
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 408..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 429 AA; 46391 MW; AB0CBC8AA7FD7023 CRC64;
MALTVAVATW LPQPHATIQD GLISAQAAEL IARDLRRELE RDPTQSIAEL AKGYELDQAP
IQTVYIVTPD GLDVLGRSLP DAVAELASSP GDPQQAARNI SRRLHVQDDG LAGYRVIVFQ
GFFPLFPALA KPGGRVLLAS FAVITSAAMA MLLARFIARP VRRLRIAGRK VAAGDLSVRV
VPSVGGRSDD IAKLAHDFDL MTERIDALLQ SRHRMLRDVS HELRSPLARL QALLSIQRQS
ADTAETRRID RMEVELERLD RLIGEILDYS RMEAADGVGR HATDLVDLLQ TIIDDAALEA
EVADKGIALR APSSCVVAVE SNLVQRAVEN VVRNALKHTA KGTAVDVSLK LDAKNVRIII
DDRGPGVPDA LLARIFEPFY RVEGAQATRS SGGGIGLAIA ERSMRLHGGS ASASNREGGG
LRVELQLPR
//
