ID F7M4B9_9BACE Unreviewed; 1356 AA.
AC F7M4B9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF0127_02314 {ECO:0000313|EMBL:EGN05470.1};
OS Bacteroides sp. 1_1_30.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=457387 {ECO:0000313|EMBL:EGN05470.1, ECO:0000313|Proteomes:UP000004085};
RN [1] {ECO:0000313|EMBL:EGN05470.1, ECO:0000313|Proteomes:UP000004085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_30 {ECO:0000313|EMBL:EGN05470.1,
RC ECO:0000313|Proteomes:UP000004085};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Yandava C., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. 1_1_30.";
RL Submitted (APR-2011) 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:EGN05470.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADCL01000048; EGN05470.1; -; Genomic_DNA.
DR PATRIC; fig|457387.3.peg.2342; -.
DR HOGENOM; CLU_000445_28_1_10; -.
DR Proteomes; UP000004085; 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 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; 5.
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}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1356
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003365712"
FT TRANSMEM 789..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 842..1059
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1100..1215
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1247..1346
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1148
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1356 AA; 154124 MW; A4F5E9A94E22F835 CRC64;
MKKIVLLITI QILCMHSFVV NAQRIFSTSY TMDDGLAANR VYSILQDSCG FMWFGTDDGL
SRFDGIAFKN YYLSEYINAT TSNSVKKIFI DRRGRMWIGL DTGIVIYDSK TDTFQPFHAK
TETGEMIQTY VTDMIEDSDG EVWIATSGEG LYRFSPSDKV RLRVYRNIPG KINSISQNII
MTLQQDSKQN IWIGTYSEGL CCFDKQKNTF VTYKKSNHPN SLSDNSIQKV FEDSHGNLWI
GTFQNGLDLF DPVAKTFTNY RDRSPNNLLY HIHDIKEYRP GELFISSDNG MGIFKADKGE
IIQSDNPNLK IRTGANKFIY TIYIDKEESL WLGSYFDGIK FYSAFQNNFK YYSCSSSSTP
QSGKVINVIK EDKDDKYWIG TDDNGIFRFD AKTQEITPFR DAASIGTTYY CIHDLLVDGD
KLYAATYGRG LEVIDLKTGK VESFLNNPED STSIPSSRVF TLYKASNGCI YVGTSAGFCY
YNPEKNNFIR IGSFTGKISD IIEDYFGRIW IGTSISGLYS YNVRTQKITS YQRSDHPNSL
TKNVITTLAI DSKKQLWVGT YGQGLCRYND ETDDFTRYDH LKLPNKIINS IIPKGDLLWI
STNKGLVVYN PDTKHIKTYS KSNGLYNEQF TPCSGFESSD GRLFLGSTDG FCYFFPQDLR
ENTYNPPVIL TNMTIFGKDI QADTPNSPIH QSIGYTDEIV LKYNQSMIGF DFAALSYIAP
KENDYQYMLE GLDSEWQFTK GSNNHLSYAN LPVGEYVLRI KGTNSDKLWS SNEVQLKIKV
LPPFFRSQLA YLIYALVLLI AIMLTVWYYV KRTEKRQKER IKRLNDEKEK ELYNSKIDFF
TNIAHEIRTP LSLIIGPLEY LMKTSSINNV YGEYLSIIEQ NYKRLYALVT QLLDFRKVDT
GSYKLSYDCY RIKEIICKVS CIFELSARQK KVAIDTSSIP EELSIVIDEE AFTKIISNLL
SNALKYAKST IRITTIEKDS EIVVTVTDDG IGITDQEKTK IFDAFYQVKN NSEINKLGIG
IGLHMTRSLV QLMNGKIEVS DREGGENGVS ISVYFPKQAA ITALPQVAKR VEDTIIPENS
IEENELESTL PGEPLKKQYA IMVVDDNPEI LDFLSKILSE EYFVISASSG EEALQILEKN
NIDLIISDVM MEEMDGFELC GKIKSNINIS HVPVILLTAK TDTESKIKGL EAGADAYIEK
PFSPFHLKAQ LLNLLKKRES QQKTYASTPL SDLHSAVHNK LDEEFMNKCT EIIQNNIEDS
EFSVNTLAQE LGMSRTSVFT KIKGIIGMTP NDFIKVTRLK KACKMMVEGE YRVTEIGFLV
GFSSSSYFAK CFQKQFGMLP TEFLKKIKED PSSATK
//