ID A0A1M6ABQ8_9BACE Unreviewed; 1330 AA.
AC A0A1M6ABQ8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444350_101162 {ECO:0000313|EMBL:SHI33818.1};
OS Bacteroides stercorirosoris.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=871324 {ECO:0000313|EMBL:SHI33818.1, ECO:0000313|Proteomes:UP000184192};
RN [1] {ECO:0000313|EMBL:SHI33818.1, ECO:0000313|Proteomes:UP000184192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26884 {ECO:0000313|EMBL:SHI33818.1,
RC ECO:0000313|Proteomes:UP000184192};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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};
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DR EMBL; FQZN01000001; SHI33818.1; -; Genomic_DNA.
DR RefSeq; WP_007660855.1; NZ_FQZN01000001.1.
DR GeneID; 69506189; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR Proteomes; UP000184192; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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 Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 4.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 3.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 775..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 828..1043
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1080..1195
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1227..1326
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1128
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1330 AA; 152439 MW; 0668763D753079A4 CRC64;
MRKIILILFL GIFCLGNLWA QQIKHYNNNS GLSHNTVMCL FQDSKGFIWV GTKNGLNRFD
GHDFKVYQRG DSINELRNSM IYCITEDKDK TLWIATDKGI SLYDPFTETF SNFNKQTDKQ
ERVDGFINKI YIDKSDRVWI LSGDGLFIYQ PSEDKLYNMH DRFAPYTAYA PRALFLDEDG
TAYLAFPDIG VIKYDIDGDK TTFLARNDNT PTAICAYKEQ YILLGTLDKG LFLINKETGE
SKKLQIDESR NSDIYVRHIE KISKDEYWVG AESGIYVLKD GAVQHITYEA YNDLSISDNA
IYALFKDREG GIWVGSYFGG VDYIPKQYSY FENFYPIAYK NSISGYRVRE FVSDRKGYLW
IATEDNGLNY YDTHTGLFTH ISDKTKPVNI SFTNIQCLNL VGDKLWIGTF TKGVDVLDLK
TNHCRHYEKD GHPNSILNND IFAIYTDSRN TTWVSSTTEL YTYVPEIDGF KVFMPMNGMF
ISDILEDKNG NIWFTTYNLG VARYNPDTKE IKRFRHDVKN PNSLCYDRIT CAFEDSKKRL
WFASEDGGFC RYNETDDTFT RITTKQGLPS NVVYKILEDD HQHFWLSTSN GLANFNPETM
SVEALYNLPN GLRSKQFNYN SGIKTEDGTL YFGSIDGFVA FNPKNFHPNE NKYSVVLTGF
YIFNQEVQVG TSDHVLDKAI PYANTINLNY DQATFSFSFS ALNYSTEGNG KYAYMLEGID
KKWNYVDNIF RIAYNSIPPG DYILHIKYSR DGHDWSDTNT VVNINIIPPL WRTSWAYALY
TLLILGMSFG VIRFYVRKKK RQVDEKMAHQ EQQKKEEIYK AKIDFFTNVA HEIRTPITLI
KAPLDYILTS HPDEHETKEN LITMERNTDR LLVLVNQLLD FRKIESKAFT LSLKIRNINV
LVANTFNRFV PTGKRKKLEM ILECPDHAVM ALVDEEAITK VCSNLFNNAI KYSSTYIKAI
LSVSEDGRIF RITVKNDGTP IPPDMRERIF EAFFQIKGAH PTQPGSGIGL TLASSLVQLH
NGQLYLDEEA EDTSFVVEIP TNASADAQQA EEDVLIEDAI TDEDNISTVV LEDSFSAKET
ILVVEDNEEL QSFLSVQLSR YYKVLTANNG EEAMEVLKGD IVNLIVSDIM MPLKDGLELC
NEIKSNLETC HIPIILLTAK TTLNNKIEGL NSGADAYMEK PFAMPHLLVQ IKNLLENRSK
LRQNFANSPY IATNSMVQNK ADEDFLNKLT EVIRQNLDDD TFNIDDLARE VNMSRTSLHR
KLKGITELTP GDFIRIIRLK KAAELLLEGE YRINEICMIV GIRSLSYFSK SFQKQFGVLP
KDFAKSHVKQ
//
