ID K6YTX0_9ALTE Unreviewed; 437 AA.
AC K6YTX0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GARC_3204 {ECO:0000313|EMBL:GAC20163.1};
OS Paraglaciecola arctica BSs20135.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC20163.1, ECO:0000313|Proteomes:UP000006327};
RN [1] {ECO:0000313|EMBL:GAC20163.1, ECO:0000313|Proteomes:UP000006327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BSs20135 {ECO:0000313|EMBL:GAC20163.1,
RC ECO:0000313|Proteomes:UP000006327};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC20163.1}.
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DR EMBL; BAEO01000047; GAC20163.1; -; Genomic_DNA.
DR RefSeq; WP_007621792.1; NZ_BAEO01000047.1.
DR AlphaFoldDB; K6YTX0; -.
DR STRING; 493475.GARC_3204; -.
DR eggNOG; COG2205; Bacteria.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000006327; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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 PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR PANTHER; PTHR45436:SF14; SENSOR PROTEIN QSEC; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 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:UP000006327};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 232..436
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 437 AA; 47926 MW; 1C4411544D5D0738 CRC64;
MSLRLRLTLL IASVFLGLWL ISSFWLITGL RSELDMALDQ RLQSTAAMLS NILATVPKNE
LGQIIPSILQ GNELGNAKGL SCQISSLHGT VIASSNTHSL PINTALSDGF GFLSSEYGQW
RTYTLKTNNI VITIADKISE RESLGFRLLE STIIPPAIAL LASLSLLWVA IGRGLLPIRK
LAVAVEKRGS TDLSPVQLDK PSQELQPLIT SQNALMARLS EGMKREQQFT NNAAHELRTP
LAGILAQIQL AELSASEARE KALSQAKASA QRLNSVLENL LALARLESEK EVAPVISWTL
NSLIDQVQRE FVSEKHRIIY NIIDEHVITF ITQPLLAIVC RNLLENALKY SPVKTEIIFL
AESTTEGITV SVRNAGNVCQ ADIPHLTSRF WRKGERQGAG LGLSILDAIA IKYKGTLVLK
NTDSSFLVTF ALPIYKD
//
