ID A0A2I9DG88_9FLAO Unreviewed; 572 AA.
AC A0A2I9DG88;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=divJ {ECO:0000313|EMBL:GBF18277.1};
GN ORFNames=C21_00434 {ECO:0000313|EMBL:GBF18277.1};
OS Arenibacter sp. NBRC 103722.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF18277.1, ECO:0000313|Proteomes:UP000095208};
RN [1] {ECO:0000313|EMBL:GBF18277.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF18277.1};
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:GBF18277.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF18277.1};
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:GBF18277.1}.
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DR EMBL; BDGL02000002; GBF18277.1; -; Genomic_DNA.
DR RefSeq; WP_051891798.1; NZ_BDGL02000002.1.
DR AlphaFoldDB; A0A2I9DG88; -.
DR Proteomes; UP000095208; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 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; 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; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF24; SENSOR HISTIDINE KINASE RPPB; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:GBF18277.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000095208};
KW Transferase {ECO:0000313|EMBL:GBF18277.1}.
FT DOMAIN 196..242
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 360..572
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..68
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 6..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 65484 MW; 20C2E58B9E5B0146 CRC64;
MVDKGSHSSN LRSKAEAKIS TTPSGGPELT IEEAKELMHE LEVHQVELEM QNQELREAQH
RLEDIRDQYT DLFDFAPIGY IILNEKGEIE NINLTACSLI GIDRTKILKR ALSAFMGANE
AHVLFIKLKE AFQNGILKPF ELEINRNNSG SFHALVQGSI TKNIKGLLQC RLSMQDITEV
RQARIIQRQH KALQSEKEKI QQYLDLAPVV FILLDKDHKI QMINQKGCDL LGYDRVELLG
QNWFDFLICK ENGKEYDPSL IDFERKIKLL APELECKVRY KNREERMMSW HNTTLLGKNG
DQIGVLSAGE DITVRTKLDE EKQIYTDNLE LKIKERSKEL IKALEAEKRI NDLKSNFITI
ASHELRTPIT IVMSSIILIE RYNSLGQYDK SNKHIARIKS SVDHFVNILD DFLSLHQLDK
GIIQIHKEVF DLEPFIQNIV TDMKGLLKKG QRIYYRHTGS KRLNLDPKIL RNIILNLLSN
ALKYSNDQIN IKSALRTDHL TITIEDQGLG IPEEDQKNLF TSFFRASNVE HIQGTGLGLS
IVQRYLELFG GNIQFKSVLG KGSAFTIVIP IS
//
