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Database: UniProt
Entry: A0A1T1HDR2_OCELI
LinkDB: A0A1T1HDR2_OCELI
Original site: A0A1T1HDR2_OCELI 
ID   A0A1T1HDR2_OCELI        Unreviewed;       549 AA.
AC   A0A1T1HDR2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BTA35_0200100 {ECO:0000313|EMBL:OOV88001.1};
OS   Oceanospirillum linum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oceanospirillum.
OX   NCBI_TaxID=966 {ECO:0000313|EMBL:OOV88001.1, ECO:0000313|Proteomes:UP000190064};
RN   [1] {ECO:0000313|EMBL:OOV88001.1, ECO:0000313|Proteomes:UP000190064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11336 {ECO:0000313|EMBL:OOV88001.1,
RC   ECO:0000313|Proteomes:UP000190064};
RA   Trachtenberg A.M., Carney J.G., Linnane J.D., Rheaume B.A., Pitts N.L.,
RA   Mykles D.L., Maclea K.S.;
RT   "Draft Genome Sequence of the Salt Water Bacterium Oceanospirillum linum
RT   ATCC 11336.";
RL   Submitted (FEB-2017) 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:OOV88001.1}.
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DR   EMBL; MTSD02000001; OOV88001.1; -; Genomic_DNA.
DR   RefSeq; WP_077242411.1; NZ_MTSD02000001.1.
DR   AlphaFoldDB; A0A1T1HDR2; -.
DR   STRING; 966.BTA35_0200100; -.
DR   Proteomes; UP000190064; 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; 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; IPR033414; Sensor_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF56; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF17149; CHASE5; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OOV88001.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190064};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        17..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          175..230
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          300..544
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          232..291
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   549 AA;  62682 MW;  5B18042ED35F5125 CRC64;
     MQRIKTFYHH NPLGVRLLAA ILIYSSLITL FATGFQLWSD YRYERSDIDK RLYQIETSSI
     RSLSNSLWEI NPAQVQIQLD GLLQLPDVRY LEITTPYGEA FFAGSKPESG QLLQHNYTLT
     HQDHNDKSHT VGKLTLIVSL EDIYQRLADK VLLILATQGV KTFLVSVFIL TLFHHLITRH
     LSTMALFARR LKLDHLDQTL ELKRGPHNDE LNDVVSAFNS MRRTMLDDIK KRQQAERALE
     SANEALADLN KQLEQRVAKR TEQLEDRNRE LQQTLNQLQN TQKQLVESEK MAALGELVAG
     VAHEINTPIG IGFTAATFLA DEAKRIEARS DAEKSDPDSK KLLALTLESS DLICRNLERA
     AQLIRAFKQV SVDQSSEQRR RFDLISYLHE ILVSLQPRLK NCRPKIQITG PNQLIIDSYP
     GSYYQIFNNL IINSVIHGFE QQPGGEINIS IILLTETKQR VEAVQQADFI QIDYTDNGVG
     VQEGWHQKLF EPFVTSKRHQ DCSGLGMHIS YNIVHQLLRG QIKSLPVQRD NPGAHFRLTL
     PVKLQPDKS
//
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