ID A0A0A2MEU9_9FLAO Unreviewed; 786 AA.
AC A0A0A2MEU9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-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=Q764_01425 {ECO:0000313|EMBL:KGO90809.1};
OS Flavobacterium suncheonense GH29-5 = DSM 17707.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1121899 {ECO:0000313|EMBL:KGO90809.1, ECO:0000313|Proteomes:UP000030121};
RN [1] {ECO:0000313|EMBL:KGO90809.1, ECO:0000313|Proteomes:UP000030121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GH29-5 {ECO:0000313|EMBL:KGO90809.1,
RC ECO:0000313|Proteomes:UP000030121};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) 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:KGO90809.1}.
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DR EMBL; JRLW01000001; KGO90809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2MEU9; -.
DR STRING; 1121899.GCA_000430025_01155; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3452; Bacteria.
DR OrthoDB; 5522855at2; -.
DR Proteomes; UP000030121; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.350; CHASE domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR006189; CHASE_dom.
DR InterPro; IPR042240; CHASE_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF03924; CHASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM01079; CHASE; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50839; CHASE; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 111..200
FT /note="CHASE"
FT /evidence="ECO:0000259|PROSITE:PS50839"
FT DOMAIN 377..429
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 430..503
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 506..557
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 575..786
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 580..607
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 786 AA; 90503 MW; 3C046A0A2877E926 CRC64;
MSIEKKITSL SSWFVSRPKT SGILVFILVL FVLNLTLFFR YQVVKKNRQF EMENLLTIVH
QNIEQTLKNS YATTTGMALT IDDNGIPKNF EEAGKQLLSY NTSIDAVQLV PDGIIKYTYP
EKGNEAAANF NILTSPLHKD AAMKAIETRK MYYVGPVELK QGGMGIVGRL PVFKKGKFWG
FSAVVIRFST FMRAAGISSL HDDRFYFQLS KTDLKTKTEQ FFLNESSDFK DKNFKSVSIP
EGDWKLYIIE KSDTALIKEF IPVLFLTFIL SIISGMLVNI VLRRPYELEN LVKIQTEKII
KNELLFKSLF EHAGLGITHT NSVNGTFIDA NDKFCEQIGY TQEEIKTMDF MMITHLDDLE
ADLKQMERLR NGEIDGFSLE KRYFHKNGSI IWVNITVSPL WTKNEKPSSH MTIVEDITKR
KQVEQDLLLS KQNIQSLINT VDGIVWEGYP DKPGVTFVSE KSKDILGYTA EEWISDDNFW
YDHLYPEDRE WVTKFSKECA EKKQPHTWEY RMINKAGNVV WVRDIVSIFI ENDESFKFRG
ILIDISKTKQ FELDLNHSVQ LLTEQNKRLL DFSHIVSHNL RSHTSNIESL TNLIEESQDE
NEKKELLGLL KKVSEALTET MDNLNDVVSV QTDINRSIEL LNLNEYIRKT ENILSNQIMK
KNATILNTIS DDCNVKYNAA YLESILLNLI SNSIRYSHPE RNPVIELKTY EENDYLVMCV
KDNGIGIDLK KNGHKLFGMY KTFTDNPESK GIGLFITKNQ IDTMQGKIEV ESEPGTGTVI
KVYFKR
//
