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Database: UniProt
Entry: Q07ZH0_SHEFN
LinkDB: Q07ZH0_SHEFN
Original site: Q07ZH0_SHEFN 
ID   Q07ZH0_SHEFN            Unreviewed;       466 AA.
AC   Q07ZH0;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Sfri_2754 {ECO:0000313|EMBL:ABI72594.1};
OS   Shewanella frigidimarina (strain NCIMB 400).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI72594.1, ECO:0000313|Proteomes:UP000000684};
RN   [1] {ECO:0000313|EMBL:ABI72594.1, ECO:0000313|Proteomes:UP000000684}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI72594.1,
RC   ECO:0000313|Proteomes:UP000000684};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA   Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT   "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL   Submitted (AUG-2006) 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};
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DR   EMBL; CP000447; ABI72594.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07ZH0; -.
DR   STRING; 318167.Sfri_2754; -.
DR   KEGG; sfr:Sfri_2754; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_133_5_6; -.
DR   Proteomes; UP000000684; Chromosome.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   CDD; cd00075; HATPase; 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   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; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF56; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 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; SSF55781; GAF domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABI72594.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000684};
KW   Transferase {ECO:0000313|EMBL:ABI72594.1}.
FT   DOMAIN          233..466
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          183..214
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   466 AA;  51854 MW;  7DF127B82BE87D40 CRC64;
     MNLHKAHIKP KIMNQNLEQV LLAVSQSELI DTGDLDSASK LIIDSVCRGL DIDRAGIWLL
     TEDNQSIGCF LLVDNQTKQN NITLTRLEFP GYFRALDTER TIAASDAMTD PATCEFKDIY
     LRPNAITAML DSPIRHAGKM IGIVCCEHKG GIRHWSRDEQ SFVSSLADLY GRAVNAKKVK
     AYQNELELNN VALEAEVEKR TAELKNAINN LQATQASLIE SEKLAALGNL VAGVAHEVNT
     PLGISVTSTS HCIDELTKLK TLFAAGELEQ QDFEEFIHTL TDGLHLIERN LSRAAELVHN
     FKRTAADQLI LEKEQVNLTE YLEQISSPLR PLTRKQGIEL DIQIEPDLVV ESYPGAIAQI
     FTNLVSNCFR HAFPADFVGQ KRIILGANYC GDEIKMFYKD NGKGLSPEVK RRIFEPFFTT
     ARNIGGTGLG MSIVYNLVTQ KLGGRLEIIS ELNQGLEIDI YIKNIT
//
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