ID A0A108TE93_9BACE Unreviewed; 1364 AA.
AC A0A108TE93;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=F2Y81_09410 {ECO:0000313|EMBL:KAA5419606.1};
OS Bacteroides cellulosilyticus.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=246787 {ECO:0000313|EMBL:KAA5419606.1, ECO:0000313|Proteomes:UP000448877};
RN [1] {ECO:0000313|EMBL:KAA5419606.1, ECO:0000313|Proteomes:UP000448877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A6 {ECO:0000313|EMBL:KAA5419606.1,
RC ECO:0000313|Proteomes:UP000448877};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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:KAA5419606.1}.
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DR EMBL; VVYV01000013; KAA5419606.1; -; Genomic_DNA.
DR RefSeq; WP_007216906.1; NZ_VVYV01000013.1.
DR STRING; 246787.BcellWH2_02366; -.
DR GeneID; 66306275; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR Proteomes; UP000448877; 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; cd00075; HATPase; 1.
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; 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; 3.
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; 2.
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; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
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 802..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 856..1071
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1116..1232
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1264..1364
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1165
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1364 AA; 156205 MW; D316BCDBA9BB3AC0 CRC64;
MENIQKVSLL FILSLLISSF QNIQGKEHKI EFKSLPPYIN IPTDVQQIYQ DRDGFIWFAT
RNGVCRFDGY ELEIIKSNLY TPGALSSNDI LAIQEDYQHR LWIGTSYGLN MLDKKSGKIQ
KEFGALNNER VQSILITKDN TIWLGTGSSL YKSNNDPEQS NTSISFTKVR SMDVKSLVEA
PNNQIWIGTW SDGLYRYITA TDSLVSYPAI NPLNSAYFLF QDSKEQIWIG TWGYGLYKLH
HPYDQEKAYF EKFAHEEGNS NSLIHNLIYS ISEDSSTGNL WIGTLEGLSC FNGKDFLNYT
PNIPSNGLPY NEIISIFRDR TGTMWLGFLG GRVYWVRPQN LQFNLHQLSH ASVGTACSNI
QGLTVYKNDL WIGLEKHSFI IHDRTTNSNS KREKAFNPSI LQSEYTYYSF LKPRHKDELW
LGSYGNGVYI YHPEESGKPL SNMRSPEIPH FPNFIYCMFE DNRQNVYLGS TTGLSILTKE
GKFYHYNNLL SPQGQYSHSV YSITQDSLNN IWIGTDHSGI FRINPTQDLS NCTFSSYSIN
NNKINSNEIQ CIFVNKEGNI LAGTDGGGLN LYDPHLDSFI SIHTQYNIPG DMICSILEDK
QQNLWMGSNV GLIKLNLKDS IAESKCRLYT TSDGLQDNKF ARGAACQAED GEMFFGGPQG
YNSFYPEKLT ADELQPDIFI TDIQVQNKSV KDLPAKDKLN IMSDLAPGYA QTLHLNYKQN
DFTCKLSVLN FYNPEKNEYA YRLDGLDHTW QYTTDRSNII SYSNLESGTY TLYIKGTNGN
GKWSKVEKAL TIIITPPWWN SMWAYIAYAI FLIAVIAYTI HFIRKRIRLK NTLRIKEVEQ
RKQEELNRAK LQFFTNITHE LLTPLTIISV TLNEIKSIAP QISDYYSIMD NNINRLKRLL
QQILEFRKAE SGNLKLKVSQ GNIASFIRKS VDSFLPLLRN KKMQLDMSIE QEEIIGYFDP
DKVDKILYNL LSNAFKYNRE GKTIRVNVSY GSSKREIIIS VSDNGEGISK ENLSKLFNRF
YEGDYRKYHT TGHGIGLSLT KELAVLHHGK IEVESQINEG TTFRVTLPII EEEFTEEEID
RSILPLPETV SDSLSVISSL NKEETIEITE KIDKKKLLLV EDNEDLLKVM ADSLSREYHI
IKATNGKEAI EQLEKTKDIV VVISDVMMPV MNGIELCHYM KKQDEWLHIP IILLTAKSSE
SDIIEGYEAG ADDYITKPFQ LTLLLVKIKS LLKNKENLLK NYSNIIAFEM QKPNIDSADK
EFLQQAINCV YEHLDDIKFD QQAFADAMRV SKSTLYRKLK SLSNEGPSVF ISDIRLQTAY
KILSDNPSMR ISDLAYTVGY NDPKYFSSCF KKKFKVLPRD ISQE
//