ID A0A0C1J010_9BACT Unreviewed; 563 AA.
AC A0A0C1J010;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OI18_02670 {ECO:0000313|EMBL:KIC96089.1};
OS Flavihumibacter solisilvae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1349421 {ECO:0000313|EMBL:KIC96089.1, ECO:0000313|Proteomes:UP000031408};
RN [1] {ECO:0000313|EMBL:KIC96089.1, ECO:0000313|Proteomes:UP000031408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-3 {ECO:0000313|EMBL:KIC96089.1,
RC ECO:0000313|Proteomes:UP000031408};
RA Zhou G., Li M., Wang G.;
RT "Genome sequence of Flavihumibacter solisilvae 3-3.";
RL Submitted (NOV-2014) 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:KIC96089.1}.
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DR EMBL; JSVC01000002; KIC96089.1; -; Genomic_DNA.
DR RefSeq; WP_039136895.1; NZ_JSVC01000002.1.
DR AlphaFoldDB; A0A0C1J010; -.
DR STRING; 1349421.OI18_02670; -.
DR OrthoDB; 9813151at2; -.
DR Proteomes; UP000031408; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 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 Gene3D; 3.30.450.20; PAS 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; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KIC96089.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031408};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 165..217
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 226..271
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 345..561
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 563 AA; 63477 MW; A3FE73D4C01F3763 CRC64;
MRIKTKLSLG LGFLFLLILL FSVLSIFHIN KLKNDANVVL KNNYESLVYC NNMLRASEEL
SLNASSLDLF ESNLAKQENN VTEPGEKEAT MALRVGFEKY RQNRDINEIN GLRNHLYQLE
ALNQHAIQRK NEIATGTAEK ANIWLSVLFT ILTLIAFSFV LNFPSVISRP ISALAEGIAE
ISRKNYRKRI YLKQGDEFGE LAETFNRMAE KLDEFESSNL ARIKFEKKRI ETIINQMRDG
IVGLDERKHI LFLNEVAQKM IGLKEPEIVG KYAPDLAVHN DLMRTLLQEN GSSELKIYAD
GKESYFMKDM LDVKDEEEIV GHVIVLRNIT PFHELNEAKT NFIATVSHEL KTPLAAIRMS
TKLLNDKRVG STNNEQQELI QSIGDDTDRL LKITSELLNM AQVETGNIQL RMQSVSPKKI
AENAIHAVNS SAVPKGVNIN FNEQQLLPLV YSDEEKTTWI LVNLLSNAIR FAPDNTTVEL
KITAENGEVV FSVTDHGKGI DEKYQPRIFD RYFKVPGETK SGTGLGLAIS KEFIEAQNGH
ISVVSNPGEG STFFVRLPAA TDR
//
