ID A0A1V9EPK8_9BACT Unreviewed; 1236 AA.
AC A0A1V9EPK8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A4R26_31820 {ECO:0000313|EMBL:OQP47825.1};
OS Niastella populi.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=550983 {ECO:0000313|EMBL:OQP47825.1, ECO:0000313|Proteomes:UP000192276};
RN [1] {ECO:0000313|Proteomes:UP000192276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=208 {ECO:0000313|Proteomes:UP000192276};
RA Chen L., Zhuang W., Wang G.;
RL Submitted (APR-2016) 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:OQP47825.1}.
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DR EMBL; LWBP01000240; OQP47825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9EPK8; -.
DR STRING; 550983.A4R26_31820; -.
DR Proteomes; UP000192276; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 2.
DR CDD; cd00130; PAS; 2.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 6.10.250.690; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF00512; HisKA; 2.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 2.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 2.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000192276}.
FT DOMAIN 326..542
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 604..719
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 805..858
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 859..898
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1013..1231
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 979..1006
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 652
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1236 AA; 139498 MW; 3CF97216D5D117D6 CRC64;
MGQRVKEFDW SRTPIGAVNS WPQSLRSALS ICLNSNFPIA IYWGRELTLI YNDAWSSIPG
NKHPWALGRA AREVWPDIWN DIEPQFDKAF SGYPGGSKDA LLPMQRHGYT EECYFDFTFT
PVYGENGKVD GVFNAVIETT YRVINERRTA FLKNFILHIA AAQTVVEVED LAIQLLKAGS
ADILFALLYN CQNEHFLLNG TTFHNESIEI CDPHNWPLDQ IVESGQPLHI NDLKVYFTAV
PKGYWEEEPT EAFIVPIKSG TRPLKSVLVC GISARRKFDG DYRVFIESIV AAIVTALNNI
YSLEEERQKA ASLAVLDKAK TTFFSNISHE FRTPLTLLLG PIEDAMNDPS TTTQNKARMD
VAYRNALRMQ KLVNTLLQFS RLEAGRVQAR FSRVDICSLT REQAGSFRSA IEKAGMQLVL
TCSEIWQEVY VDVEMWEKIV MNLVSNAFKY SKQGCITVSI TGADHSVRLS VSDTGIGIPA
DQLQKIFDRF HRVDNVEGRS QEGAGIGLAM VKELVHLHNG TITVESQPGK GSTFTVTIPG
GKEHLPADKI DDTVAPISVS HQADAYIQEA MKWLPEDDQK NNELHDIMLD EGFQTYASST
TNTRVLIADD NADMGEYLQR LLRNYYEVLT ATDGEDAFIK ALKYKPQLII SDIMMPRLDG
FRLLNYIRAH AVTKNTPVIF LSARAGEEAK VEGLDAGADD YLVKPFSSKE LLARVEANIR
LAKNRQAAEN NLRSVIMQSP VATTLLRGPS FIIDIVNEKG LEVWGRRYHE VINLPIAQAL
PEVEQQGFVK LLEQVYNTGV PFNGDEVPVD LVRFGRPETI YLNFIYTPVR DEENRVYGVL
GIGVDVTAQV IARKKIELSE SKLKEMANAM PQLVWVTNSE GQVTYFNDRL SEYGGVQKLA
DGNWFWQGLV HDDDLVRAQQ IWERAVAAGD AFQFEHRIQM KDGNYMWHLT RGVPHKDREH
GTVQWFGTTT NVHITKEQAS LLEQQVQART QELKELNLSL QKSNQELQQF AHVTSHDLKE
PLRKIKTFLG RIIDDDRTYL SDISKVYAAK VKAAADRMKA MIEGVLNYST IEAEQQELEP
VDLTEVIQQI EADLELEISR KSATLEYERL PIVEGASVLF YQFFYNLLNN SLKFSQPDVL
LHIVINHTLV KKDGGEWAEI TVRDNGIGFE QQFSEKIFET FSRLNSKDRF EGTGLGLSLC
KRIIERYGGT VKATGEPGKG ARFLITLPLH QTKASH
//
