ID A0A2I9E2A9_9FLAO Unreviewed; 524 AA.
AC A0A2I9E2A9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=walK_2 {ECO:0000313|EMBL:GBF21504.1};
GN ORFNames=C21_03690 {ECO:0000313|EMBL:GBF21504.1};
OS Arenibacter sp. NBRC 103722.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF21504.1, ECO:0000313|Proteomes:UP000095208};
RN [1] {ECO:0000313|EMBL:GBF21504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF21504.1};
RA Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL Genome Announc. 4:e01155-16(2016).
RN [2] {ECO:0000313|EMBL:GBF21504.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF21504.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:GBF21504.1}.
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DR EMBL; BDGL02000020; GBF21504.1; -; Genomic_DNA.
DR RefSeq; WP_031444513.1; NZ_BDGL02000020.1.
DR AlphaFoldDB; A0A2I9E2A9; -.
DR Proteomes; UP000095208; 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 InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
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:0000313|EMBL:GBF21504.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000095208};
KW Transferase {ECO:0000313|EMBL:GBF21504.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 306..524
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 524 AA; 60229 MW; 6A9837337649C09D CRC64;
MNKRLFGLLV VLMSLSLIGI IFVQSYWINK SVADKEEQFS NTINQILSRV VENIEKREVQ
DYLNEFYKLK DSIGKPKATH LKNFFFFDRD INSNEIRFYT HGILEEDYNM ASTFFDIGLD
TTTFRNITST RTTEIYKEDF GLDGRQYSLT PVQKLEKIGG LSSIDKAALD DVFREQAKSR
SIHKRVSKQE IELFLGRELK NRGIDIDYEY GVYSKGLPTK VKSKKFKFTE TTLYKAPLFK
DSEGNTNFSL LLTFPKKKRF LIQSILGMAI LSLTFTLVIV VAYSSAIYQL IKQKQISEIK
SDFINNMTHE FKTPIATINL AVEAIKNPKI IDDKEKVLRY LQMIRDENKR MHAQVENVLR
ISKLEKNQLD ISKDRADIHD IIEDAITHVE LIVADRGGYI KPHLKAERSE VLANEMHFTN
VIVNILDNAV KYSPEVPKID VFTEVVGNYI IIKVQDQGAG MSKAVLKKVF EKFYREHTGD
IHNVKGHGLG LAYVKKIVDD HQGEVYAESE KGKGSTFYIK LPLI
//