ID A0A069D5A6_9BACE Unreviewed; 1370 AA.
AC A0A069D5A6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=JCM15093_2744 {ECO:0000313|EMBL:GAK37491.1};
OS Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK37491.1, ECO:0000313|Proteomes:UP000027601};
RN [1] {ECO:0000313|EMBL:GAK37491.1, ECO:0000313|Proteomes:UP000027601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK37491.1,
RC ECO:0000313|Proteomes:UP000027601};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
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:GAK37491.1}.
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DR EMBL; BAJS01000021; GAK37491.1; -; Genomic_DNA.
DR STRING; 1121097.GCA_000428125_02298; -.
DR eggNOG; COG3292; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR OrthoDB; 717811at2; -.
DR Proteomes; UP000027601; 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; 3.
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; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:GAK37491.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027601};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1370
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001659965"
FT TRANSMEM 771..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 825..1061
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1103..1218
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1251..1350
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1151
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1370 AA; 156600 MW; 7AE15F1C65279C0B CRC64;
MKAPWFILLL YILVSCHAVD KSKEQESELQ SLVIASDLSN QQIKSIAEDA QGHIWIGTFR
GLNKFNANEY HQYFCADDSL GLPDNQIQDI LLDSKKQLWI ATVNGVCQYT DQDNFVHIPI
NASNKNMVQL IENKEGRMFF NAVLQLYAYN PLTKSIDCVI PNLDPNHTFN VRCYVDDNDK
LWVVSPRALV CYDSSTLVLK DSISLKGTPS YSFMHNKKEL WLTGNHTIAI FDTQTHQFKE
LPQAIKQHPL LSNANIEYIH PYGDNSLLIN TSKHGMFYYN FIDNTVTHQE EDGFPFEVPH
FKISKIFTDS QKNLWFGSLD QGISVSYHYK ERFNNNNYLR SALENKSVVS IAAEKNHNIW
ISTLMNGLYV YDIQNQKMEN ITIEKLFPQE KQRAIYVNQI FVDNANDIWM TATNNTVLKC
SYINGSLKIK AQYNVFYPMS ITQDHYGTMW IGTASVYLYA LKQGDTEFRP IKMYDTRFTF
IPSLLPLKSG SVLIAAFNQP MKLIDSKSLQ IKELAVSPQD MKTSIRRSVF IPTAIYEDTQ
GEIWIGTVSN GLLCYSPQTG KIRPVPGTAC LDISGIEEDK QGLLWVSTQY GLSKYDRIAD
KFSNYYAADG IGGNQFYDRS SCPLPDGTLL FGGTHGLTFF NPADIPVKRN IPILFQDLKI
DNRLIRPAKG ECIDKHLSYK PNIQLKHYQN SFSISFAAPD YCEHGRVHYH YMLENFDKDW
IDAGNNHEAY YANLPSGKYS FKVKITNNDK SIIEAEDAIQ VTVKPAPWAT WWAYSIYFII
AAGIIGSFIS IYLRIRSEKK LAQKAELEKE QERRVNKMNM SFFANVSHEF RTPLTMIAGP
VTQLCNNPEI SGDNKALLFI VQRSVERMLR LVNQLMDFHK LENDTIKLKV SKIDIISFLQ
QLVDVYRTNA KEKGITLNTF GLEDSLLAWV DEDKMDKIFG NLMSNALKFT PIGGCIEVHL
DLVNREEAGL CFALTEKDKD VQFIQISVSN TGQTIPDNKL DKIFERYYQM TNQNEGIYNW
GTGIGLYYAR SLTQIHHGYI KAGKSDNGQG VVFTFILPIN DISYEENERS KRQKSQTDAF
PLIQEKTVYM KNEDSENTEK QNSILVIDDD TEVVHYLKTL LSPYYKIIYR FDANSALQAL
KEDAPDLILS DVVMPGKNGY EFCREIKEDL QLCHIPVILV TAKATVQNQV EGLNTGADAY
VTKPFDPSYL LALISSLLRN REKVRNLLGR ATQTDKLDDN ILSPQDKSFM TNLYQLMENE
LSNPELDVAR MTEMLKISRT KFYYKVKGLT GENPSFFFKT YKLNRAAELL VEGKYTVSEI
ADLTGFSTLS HFSKSFKKQF GITLASTTKP RYFIFEREKA NYQSVISTVT
//
