ID E6SVI9_BACT6 Unreviewed; 1300 AA.
AC E6SVI9;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Bache_0474 {ECO:0000313|EMBL:ADV42499.1};
OS Bacteroides helcogenes (strain ATCC 35417 / DSM 20613 / JCM 6297 / CCUG
OS 15421 / P 36-108).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=693979 {ECO:0000313|EMBL:ADV42499.1, ECO:0000313|Proteomes:UP000008630};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P 36-108;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Bacteroides helcogenes P 36-108.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADV42499.1, ECO:0000313|Proteomes:UP000008630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35417 / DSM 20613 / JCM 6297 / CCUG 15421 / P 36-108
RC {ECO:0000313|Proteomes:UP000008630};
RX PubMed=21475586; DOI=10.4056/sigs.1513795;
RA Pati A., Gronow S., Zeytun A., Lapidus A., Nolan M., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brambilla E.,
RA Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Lucas S.;
RT "Complete genome sequence of Bacteroides helcogenes type strain (P 36-
RT 108).";
RL Stand. Genomic Sci. 4:45-53(2011).
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; CP002352; ADV42499.1; -; Genomic_DNA.
DR RefSeq; WP_013546115.1; NC_014933.1.
DR STRING; 693979.Bache_0474; -.
DR KEGG; bhl:Bache_0474; -.
DR PATRIC; fig|693979.3.peg.509; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000008630; Chromosome.
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; 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; 2.
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; 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 Kinase {ECO:0000313|EMBL:ADV42499.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008630};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:ADV42499.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1300
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003209442"
FT TRANSMEM 745..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 794..1010
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1050..1166
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1199..1298
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1099
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1300 AA; 146355 MW; E1BAC556AEC0FEFE CRC64;
MKRILLAVLV SLLSLFPQSK AAGSKQYAFQ RIDIRNGLSY SVRCLTVSHD KGYVWIGTRS
GIGRFDGYEL KKYLHDNVTH IVEDKEHTIW AITSKGLFYY NYQNDEFTQA RDNDNNPVLA
SSICLWADGV LFGGNGKLYK HSYADRRTKY LCSLMSDSKY NITGLQKWDD RTLLCTNRWG
HALFTDIATG KTRPVPFESK GLMATLIDAK GNIWVAPYHQ GVKCYDRKGR LLHSYQTQNS
PLRTNVVLSL AECDGQIWIG TDGEGIYILN PETDAMSALS HVPGNPYSLP ANSILCLYAD
SSNNMWAGSV RGGLINIKEV GIKIYADALP GIEYGLSEKT ILSLYQGDEE DIWIGTDGGG
INRFNPRTKK FHHVLPSWGD KVASITGMDE RQLLVSLFSK GLFFFDKQTE RYRPLVIVND
SINSLLCQQG KAVNLFRNTA ETVLLLSELP YSYNPARKEF TPIGGDVKNI IGTILPIYSD
GMVTYMHDFK HIYRIDARNN RLQTLYSCQG DTTLNSVSAD ENGTFWIGSN HGLSYFSPAK
KKHACIPNSL ISEITSIVCD KRGRVWIGTN DKLFAHLVYE GEFILYGEPD GVIPNEYLEK
PRLLSLQGDV YMGTVNGLLC INKHLPQDET SPPVLELADI LIGGERMNSL IIGKRSLQVG
EQSRPISIKI IAHDKDIFRK PIYRYTLRGM EGQVTYSYLP ELTLSSLPAG TYQVMAACST
RTGGWTDDYQ IMELTVLPPW YKSGWFVACC ILSAASCTAL IFLLLLRRKE NKLKWAMKEH
EQQVYEEKVR FLININHELR TPLTLIHAPL RQLLDSLSPD DDKYRTIQNI SRQSGRMKKL
LDMVLDVRKM EAGHSTLNVE TVELNPWIEQ LLADFRPEAD MKHISIVYQP DNEAESLQFD
KEKCTTILIN LLINALKYSS ENRRIYIATS LSDDKTRLRF SVSDEGPGLK GTDIDNLFTR
FYQGNNSRPG TGIGLSYSKI LAEQHGGSIG AYDHGDMPGA TFWFELPRDL QPGKVTLQPR
PYLNELLAPT QETESTPGGM PRKEDTQGRT LLIVDDNKDL TEYLSAALKG CFKETKVAYD
GEEALKICRE SPPDAVVSDI QMPRMNGYEL CKQIKEDLKI SHIPVILLTA RNDEESQIFG
YKNGADAYLT KPFDVNMLYI TIHSQLKNRE RMKVRYAGAH TPPPPQESTF SAADEKFLNL
LNKLITDNLA EERLSVPFLC SELGVSRSSL YNKLKALTGM GANDYINKMR IGRAAELLTG
STLSINEIAD RTGFSTPRYF STAFKQSMGC PPTQYREENS
//
