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Database: UniProt
Entry: A0A1W9LB34_9GAMM
LinkDB: A0A1W9LB34_9GAMM
Original site: A0A1W9LB34_9GAMM 
ID   A0A1W9LB34_9GAMM        Unreviewed;       322 AA.
AC   A0A1W9LB34;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BWK79_01790 {ECO:0000313|EMBL:OQW95646.1};
OS   Beggiatoa sp. IS2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Beggiatoa.
OX   NCBI_TaxID=1934247 {ECO:0000313|EMBL:OQW95646.1, ECO:0000313|Proteomes:UP000192324};
RN   [1] {ECO:0000313|EMBL:OQW95646.1, ECO:0000313|Proteomes:UP000192324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IS2 {ECO:0000313|EMBL:OQW95646.1};
RA   Sharrar A.M., Flood B.E., Bailey J.V., Jones D.S., Biddanda B.,
RA   Ruberg S.A., Marcus D.N., Dick G.J.;
RT   "Novel large sulfur bacteria in the metagenomes of groundwater-fed
RT   chemosynthetic microbial mats in the Lake Huron basin.";
RL   Submitted (JAN-2017) 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:OQW95646.1}.
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DR   EMBL; MTEL01000027; OQW95646.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9LB34; -.
DR   Proteomes; UP000192324; Unassembled WGS sequence.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
FT   DOMAIN          1..189
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          191..322
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
SQ   SEQUENCE   322 AA;  35442 MW;  B2E913100D6C75E4 CRC64;
     MRVRLVPIGQ TFERMRFVVR DLARETQKQV RLVLDHQEIE VDKLVADKIA DPLLHLVRNA
     ISHGLELPEE RIAQGKSSEG TIYLKASAAG DAVLIEVEDD GRGIDREQVL QQAYRQEIFA
     AGHLPDDHEF LELLCKPGFS THQQVDLTRG RGIGMDVVKN AVLELGGHIS LETQKGSGTR
     FVIQLPLTLA IADALIVAVG KQHFAIPQLS VREVIAFHSS TITTAQESEI VFHRGKPLPL
     IRLARCFGLT ENESLTVTVL VVGSLHEVGL IVERVIGRRE IVVRALNDPL VRIAGIAGAT
     ELGDGRIILV TDVGMLIKQY LV
//
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