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Database: UniProt
Entry: M7NV21_9BACT
LinkDB: M7NV21_9BACT
Original site: M7NV21_9BACT 
ID   M7NV21_9BACT            Unreviewed;       492 AA.
AC   M7NV21;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=evgS {ECO:0000313|EMBL:EMR02294.1};
GN   ORFNames=ADICEAN_02566 {ECO:0000313|EMBL:EMR02294.1};
OS   Cesiribacter andamanensis AMV16.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC   Cesiribacter.
OX   NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR02294.1, ECO:0000313|Proteomes:UP000011910};
RN   [1] {ECO:0000313|EMBL:EMR02294.1, ECO:0000313|Proteomes:UP000011910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMV16 {ECO:0000313|EMBL:EMR02294.1,
RC   ECO:0000313|Proteomes:UP000011910};
RX   PubMed=23682146;
RA   Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT   from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL   Genome Announc. 1:E00240-13(2013).
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:EMR02294.1}.
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DR   EMBL; AODQ01000064; EMR02294.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7NV21; -.
DR   STRING; 1279009.ADICEAN_02566; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   OrthoDB; 9797097at2; -.
DR   Proteomes; UP000011910; Unassembled WGS sequence.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
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   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR018060; HTH_AraC.
DR   InterPro; IPR018062; HTH_AraC-typ_CS.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
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; PF12833; HTH_18; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 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; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 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   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011910};
KW   Transferase {ECO:0000313|EMBL:EMR02294.1}.
FT   DOMAIN          1..190
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          246..361
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          393..492
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         294
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   492 AA;  54038 MW;  5ECB62D5FB6120E8 CRC64;
     MKESAARLLR LINQILDLSK LDAGQLRLSL RLTELQTLLK GVTASFSSLA DSRAIALRFT
     AQERLPALYC DPAHVETILI NLLSNAFKFS QEGGSVEVRV AVLPPALPAF PEGALDISVS
     DEGEGITQEQ LAHIFDRFYQ AGHARESLWG GTGIGLALTK ELVELHGGSI TLESRVGEGS
     TARVRLPLGS RHLSPAQLQA ATDRQGDWSL PLTAAAGLTE TLAEASATDL NATAVSAVAP
     AAVRPLLLLI EDNADVRAYI RSILAADYRL LEAPDGETGV RLAQQEITDL IISDVMMPGI
     DGYEVCRRLK QDERSSHIPL ILLTAKASVH SRLQGLEQQA DLYLSKPFVP QELRLCLHNL
     LQARLRLQER YQKQVVLKPS ELAVSSVDEA FLKRLMGVLE IHHARESFSV EQLSLEMGMS
     RSQLHRKLEA LTNESASHFI RSFRLQRAMD LLQKKHASIS EIAYMVGFSS PSYFTRCFLK
     HFGTTPSAVL EA
//
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