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Database: UniProt
Entry: A0A0F4QV74_9GAMM
LinkDB: A0A0F4QV74_9GAMM
Original site: A0A0F4QV74_9GAMM 
ID   A0A0F4QV74_9GAMM        Unreviewed;      1294 AA.
AC   A0A0F4QV74;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=TW77_06445 {ECO:0000313|EMBL:KJZ11150.1};
OS   Pseudoalteromonas rubra.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ11150.1, ECO:0000313|Proteomes:UP000033452};
RN   [1] {ECO:0000313|EMBL:KJZ11150.1, ECO:0000313|Proteomes:UP000033452}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2471 {ECO:0000313|EMBL:KJZ11150.1,
RC   ECO:0000313|Proteomes:UP000033452};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ11150.1}.
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DR   EMBL; JXYA01000011; KJZ11150.1; -; Genomic_DNA.
DR   RefSeq; WP_046004145.1; NZ_JXYA01000011.1.
DR   PATRIC; fig|43658.5.peg.1356; -.
DR   Proteomes; UP000033452; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR013783; Ig-like_fold.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR011110; Reg_prop.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR011123; Y_Y_Y.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07494; Reg_prop; 2.
DR   Pfam; PF07495; Y_Y_Y; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033452};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..1294
FT                   /note="histidine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002475859"
FT   DOMAIN          1061..1293
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          1022..1052
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1294 AA;  143237 MW;  A1BB849E6868EBF1 CRC64;
     MIRLPGLRRV VALLLLLCTY LMPFTAVTAT ETSVHPSQPA TGNSFFELGE LIFQTIGDNE
     QIPQGVVTAL AQDRDGFIWI GTQFGLLRFD GYRFVTFLHD PKDDTSLSGS FIRSLWVAPD
     GRVWIGTFAD GISVYNPATG RFKRFEHNPS DNNSLYNNTI RALSGDDQGN IYAATDNGLN
     HIEATTGRVS RLKITGCDQP LIQPRLRSLL LRGTNTLWVG SKTGLCRVTL PNGHASGEAN
     WQQPLSGETL AAFNQQNVFR LFQDANHAIW VGTTDHGAAF FMPGSDQVTR IHHRPGDPTS
     LSHHWVNGII QPDPEHIWLS TSGGGITVVN ANSGAVIRHI RHDPLNPYSI NLDSMGALLV
     DASGLIWAGT WGNGLNRHNP HNGAFRTFVR RLSYPHSLSH EDVRSITELD NGQIWVGNAQ
     TGIDIIDPSM GVVAGHRPDP GDPSKLADGY VRVIRQTFDG SVWTGSANTG LHHFDPLSQQ
     FTRYSKADGL PGYQVVMLQE TANGQLWVGT DEGLALMDIK TRQLQPLSAF KNHTLLSGKP
     VLTMAYMAPD LLWVGTRIGL LVLDLKAKTV TEISARAQTT DTLSDNYIKS LLVDSQGRLL
     VATPHGLDRL VHFDGHQAQF ESLDQLAGRP TGTAGNLMED AQGRIWNGYG WLDPSAQSFE
     DLGVADDWDT GTMWTGSYTK LRDGTLVFGG TKGILLLRPG RWRHWTYHPP LVISELAVNN
     QPVTVPKQLV LPPSTRSFSV EFAALDFTAP HSNRYAYQLV GYDEQWIPVD ASKRHITYTR
     LPPGHYQLKI KGSNRKGQWS QHQLNLAVIQ LPAWYETWWF RLGLLLLITS LLYLAYLWRI
     KELKQQQVAL DNLVQSRTAN ISMLGTIGKD ITSTLDLSSV LERVYKHVNE LMGADVFVVG
     ILDRENQRIS CRLAIEKGQK LPEFEYALSD TQRPAVWCVT QQKELRVNQI SELTQYVDHI
     AAPVSGAESE SLVYLPLIID TRIIGCLTVQ SFQPHAFSDN DVQMLRTIAN YTAIALANAD
     AVAQLESTFN QLQTAHEDLK VTQQQLVQQE KMAGLGRLVS GVAHEINTPL GIGITAGSYA
     SKALAECEQK LASGKLSKDH LEQFFATLQE SLQLLESNLG RAAQLVKNFK QVAVDQSIEE
     LSTINLPDYL NDVLTSLHPK WKHTQVTVKT DFPSEARLST YPGAIAQILT NLVDNAIKHA
     FDEGTQPGTI RITIKDTPEQ LTWIVTDDGA GMSEETRDKV FEPFYTTRRS HGGTGLGMHI
     VFNIVTQKLK GTIECHSEPD QGCQFTLVLP KSSD
//
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