ID A0A0M7BGG8_9RHOB Unreviewed; 729 AA.
AC A0A0M7BGG8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=srrB {ECO:0000313|EMBL:CUH40436.1};
GN ORFNames=JSE7799_03168 {ECO:0000313|EMBL:CUH40436.1};
OS Jannaschia seosinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=313367 {ECO:0000313|EMBL:CUH40436.1, ECO:0000313|Proteomes:UP000049455};
RN [1] {ECO:0000313|EMBL:CUH40436.1, ECO:0000313|Proteomes:UP000049455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7799 {ECO:0000313|EMBL:CUH40436.1,
RC ECO:0000313|Proteomes:UP000049455};
RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL Submitted (SEP-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CYPR01000207; CUH40436.1; -; Genomic_DNA.
DR RefSeq; WP_055664483.1; NZ_CYPR01000207.1.
DR AlphaFoldDB; A0A0M7BGG8; -.
DR STRING; 313367.JSE7799_03168; -.
DR OrthoDB; 9776727at2; -.
DR Proteomes; UP000049455; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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 Gene3D; 3.30.450.20; PAS 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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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:UP000049455};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CUH40436.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 312..365
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 502..726
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 729 AA; 81022 MW; A2AC87DDC1259D15 CRC64;
MFLWERRRQI QSGIAVVLVV LGPALVVLTF LALSVRGPSG DLTWLRGVLL FDAVYILAVA
ALVVRRLTRM IAARRARSAG SQLHLRLTGV FTGIALVPTI LTAVFATVTI NIGLEGWFSD
RVRNALGNSV EAAQAYAQEV RDGLTEDARA LGSYLDVAKR AAFFMDDGNL REVLADGQAQ
IQRGLEEAFV VDGAGEIRAR GERSYLFDFE PIPPERLDQA ENGSVILIED KEINEFRVLL
KLDAYPDRYL YVTRAVDGDI LQLLDETRAT AQLYQQLERD RGRILFEFAL LYLGFALILI
LAATWAGLWF AERLSRPVGR LAGAAQRVGQ GDLSVRVTEE DGDDEIAMLG RIFNQMTRQL
KGQRDALVET NMQTERRRRL FDSVLGSVTA GVIGLDPDGR IDFMNRSAQR LLVLDEERYG
VDLGRVVPEF ATVLSRLQET HADTMQEEIR LTRGGKLESL LVRIATRPGA DEAPEGYVVA
FDDVTDLVSA QRMAAWGDVA RRIAHEIKNP LTPIRLSAQR VNRRFGKELS PESAAKLGEL
TDVIVRQTGD LGRIVDEFSR FARMPEPERR RGDLAALLRE TVTLQRAALD PIELVATIPD
GPLPAEFDHT MMGQAFTNLV KNAGEAIETR EEKLDAPFEK RVKVTLETLD HHVEIRIADT
GVGLPQDRAR LFEPYVTTRD KGTGLGLPIV KKIIEEHGGT LDLRDAEPGP DGHRGAEAVI
RLPRIEEEH
//
