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Database: UniProt
Entry: K0C7M8_ALCDB
LinkDB: K0C7M8_ALCDB
Original site: K0C7M8_ALCDB 
ID   K0C7M8_ALCDB            Unreviewed;       628 AA.
AC   K0C7M8;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=B5T_01201 {ECO:0000313|EMBL:AFT69484.1};
OS   Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS   B-5) (Alloalcanivorax dieselolei).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alloalcanivorax.
OX   NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT69484.1, ECO:0000313|Proteomes:UP000006286};
RN   [1] {ECO:0000313|EMBL:AFT69484.1, ECO:0000313|Proteomes:UP000006286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC   {ECO:0000313|Proteomes:UP000006286};
RX   PubMed=23144414; DOI=10.1128/JB.01813-12;
RA   Lai Q., Li W., Shao Z.;
RT   "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL   J. Bacteriol. 194:6674-6674(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};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003466; AFT69484.1; -; Genomic_DNA.
DR   RefSeq; WP_014993565.1; NC_018691.1.
DR   AlphaFoldDB; K0C7M8; -.
DR   STRING; 930169.B5T_01201; -.
DR   KEGG; adi:B5T_01201; -.
DR   PATRIC; fig|930169.3.peg.1188; -.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_104_15_6; -.
DR   OrthoDB; 9797243at2; -.
DR   Proteomes; UP000006286; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFT69484.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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        155..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          179..231
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          260..482
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          503..622
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         552
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   628 AA;  69016 MW;  AF4AE2CD79623F2E CRC64;
     MMAQGGIRRQ LRWLGVIPAL IMLVLVLVTL TWQRLQDADN EVRELGGFLA RQLAAAAEYG
     VLSGNTSELR RHANMALQRP DVYYVAFRDE TGQVLLSEGR ATSDGRGGLL EFRAGIYRQP
     LSASETERYV DPGDRVGEVV LGLAPELLAA RQKEILAASL VPALLAMMVG LVCAGYLARR
     IAEPLSYLSG LVRVIRGGDY RARGDHHLQG ELSDLQRDIN ELASGLERAR ADQQRAMGEL
     RQAHRSAQQA SQAKTDFLAM MSHELRTPMN GVLGMLQLLE TTRQNEEQRE YTQAALESTG
     HLLEVINDIL DFSRIEAGRM DIDQTFFAPG PLLENCIGTF RYVARHKGLY LELEGLEQLE
     GYDLYSDPTR LRQILSNLIS NAVKFTEQGG VRVTIQASAD EHGLMNLSLS VTDTGIGISD
     AQRDRLFVAF SQLDASPSRR YGGTGLGLAI ARRLAEMLGG DLAVKSRAGE GSCFTLRLRV
     RARAAGEQAS DGPRIDDGHL RGRALLVEDN LVNRMVAARM LENLGLEVVS CGDGETALNT
     IQGENFDVVL MDVQMPVMDG LEATRAIRRW ERAAGRSPVP IIALTANALG EERERCLASG
     MDDHLAKPYR RQLLAKLLSR YLKTAEAG
//
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