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Database: UniProt
Entry: F7M4B9_9BACE
LinkDB: F7M4B9_9BACE
Original site: F7M4B9_9BACE 
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}.
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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
//
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