ID A0A0S8K2Q5_9BACE Unreviewed; 769 AA.
AC A0A0S8K2Q5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AMS26_08120 {ECO:0000313|EMBL:KPL15237.1};
OS Bacteroides sp. SM23_62.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL15237.1, ECO:0000313|Proteomes:UP000050819};
RN [1] {ECO:0000313|EMBL:KPL15237.1, ECO:0000313|Proteomes:UP000050819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL15237.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL15237.1}.
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DR EMBL; LJUP01000058; KPL15237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8K2Q5; -.
DR PATRIC; fig|1703352.3.peg.3263; -.
DR Proteomes; UP000050819; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
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; 4.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 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; SM00086; PAC; 4.
DR SMART; SM00091; PAS; 4.
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); 4.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT DOMAIN 37..80
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 112..164
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 165..238
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 240..292
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 361..418
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 419..489
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 548..766
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 7..51
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 769 AA; 88142 MW; A4B681D0D3721807 CRC64;
MNGQPTYDEL ASIRLQLEQR IARLEEQLKQ EAELRQLEEK YKRLVESLSE EYIFYSHDRE
GMVTYVSPSI TKILGYSQEE SMRNYREFLT DHEMNQEALD RSRASLRGLV QPPFMNELYH
IDGSTRIFYN TELPIYDENG RVTGVEGIAH DVTKKYAAEE EMRKQDEILR LLVDTIEEVF
WIHDLKADQL LFISSKYEGV FGRTTESLYQ NPGSFLKSVH PEDREYVKKA YKKIGKGKGL
DMEYRIIDPS GNEKQIWTRS FVIRDDRDKP SLSIGTAQDI TQRKKSQQER DLLAAIVENV
EDHAVIKDTD LKVIASNRAN TAAAGKKSAD QLIGKTDLEI YGDFDHVRQY MEDDRKAMKL
KQGETLVNDQ VFVYPDGRKI HSLVKKFPVY DEKNKLIAVA SISRDVTDYK NTLEELYRSE
RKYRLLIDNQ GEGIGMVNQY DQFIFVNPKA EEIFGVAPGK LVGKTVFDFL SPENRKFIRD
QTELRKKGAE NTYELEIIRP DKEKRQILVT ATPQYEEGEF SGTFAVFRDM TGWKSQETTS
AKDKFISIIA HDLKNPLSSI TGFSDLLMKD YTTYDQEEVL TFVKMIHGAS RQAQNLLNNL
LDWSRSQTGR IGFEPTGIDI SQVVESVFKL YDLNVREKNL HIHNRVNRDT LVYGDQNMVS
TIVRNLISNA IKFTRPKGRI NVSAKSSRHA IQILVADNGI GIPEDLAGKL FRIDEQVTRT
GTANEEGTGL GLILCMEFAR KCNGTLTVSS KPGKGSTFTL RLPRHRPEG
//
