ID A0A0M6YN68_9RHOB Unreviewed; 742 AA.
AC A0A0M6YN68;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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:CTQ50687.1};
GN ORFNames=JDO7802_02713 {ECO:0000313|EMBL:CTQ50687.1};
OS Jannaschia donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=420998 {ECO:0000313|EMBL:CTQ50687.1, ECO:0000313|Proteomes:UP000049222};
RN [1] {ECO:0000313|EMBL:CTQ50687.1, ECO:0000313|Proteomes:UP000049222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7802 {ECO:0000313|EMBL:CTQ50687.1,
RC ECO:0000313|Proteomes:UP000049222};
RA Noorani M.;
RL Submitted (JUL-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; CXSU01000012; CTQ50687.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M6YN68; -.
DR STRING; 420998.JDO7802_02713; -.
DR Proteomes; UP000049222; 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 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; 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; PF13188; PAS_8; 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.
DR PROSITE; PS50112; PAS; 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:UP000049222};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CTQ50687.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 325..378
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 390..430
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 515..740
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 742 AA; 82093 MW; 4936CA93ABCE2E4A CRC64;
MRASASQQGA LSRPFLWSGR RQVQTILTLT LVVLGPVLVI LTFLPLGLRG PQGDLTWLRV
ILLADLVYIL AVAALVVRRV TRMIAARRAG SAGSQLHLRL TGVFTGIALI PTVLTAVFAT
VTINIGLEGW FSDRVRNALG NSVEAAQAYT QEHRDGLTED ARALAGYLNV AKRSLFLMSD
GDLRQLLAQG QELVQRGLEE AFVIDGGGEI RARGDSSYLF DFVPVESSLM QRAAEGSVIL
IEDEDINEFR ALLKLTAYND RYLYVTRAVD GEILELLDQT QETSQLYRQL EQDRGRLLFE
FGLLYLGFAL ILILAATWAG LWFAERLSRP VGRLAGAAQR VGQGDLDVRV TEEAGTDEIA
MLGRMFNQMT RQLKGQRDAL VETNTQTERR RRLFDSVLSS VTAGVIGLDA FGKIDFMNRS
AHRLLGIEGE RYGEDLDRIV PEYGDLFARL RSAPTETVQE EIRIARGGRL ENLLVRIATR
PGSDGMAEGY VVAFDDVTEL VSAQRMAAWG DVARRIAHEI KNPLTPIQLS AERLKRRFSK
ELSEDSAAKL GELTDVIVRQ TNDLRRIVDE FSKFARMPEP ERRRGDIAAL LRETVILQRA
ALDPVPIEQD IPATPVMAEF DATMMGQAFT NLVKNAGEAI ETRVERSGDD FQKSVTVHLD
DTDPTHLEIR ISDTGVGLPE DRARLFEPYV TTRDKGTGLG LPIVKKIIEE HGGTLDLVDA
VADATGHTGA QAIIRLPRIE ET
//
