(data stored in ACNUC7421 zone)

SWISSPROT: C5B762_EDWI9

ID   C5B762_EDWI9            Unreviewed;       778 AA.
AC   C5B762;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 67.
DE   RecName: Full=Aerobic respiration control sensor protein {ECO:0000256|PIRNR:PIRNR003182};
DE            EC=2.7.13.3 {ECO:0000256|PIRNR:PIRNR003182};
GN   OrderedLocusNames=NT01EI_0607 {ECO:0000313|EMBL:ACR67836.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67836.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine. {ECO:0000256|PIRNR:PIRNR003182,
CC       ECO:0000256|SAAS:SAAS00049098}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|PIRNR:PIRNR003182}; Multi-pass membrane protein
CC       {ECO:0000256|PIRNR:PIRNR003182}.
CC   -!- PTM: Activation requires a sequential transfer of a phosphate
CC       group from a His in the primary transmitter domain, to an Asp in
CC       the receiver domain and to a His in the secondary transmitter
CC       domain. {ECO:0000256|PIRSR:PIRSR003182-50}.
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DR   EMBL; CP001600; ACR67836.1; -; Genomic_DNA.
DR   RefSeq; WP_015870033.1; NC_012779.2.
DR   ProteinModelPortal; C5B762; -.
DR   STRING; 634503.NT01EI_0607; -.
DR   EnsemblBacteria; ACR67836; ACR67836; NT01EI_0607.
DR   GeneID; 7960375; -.
DR   KEGG; eic:NT01EI_0607; -.
DR   PATRIC; fig|634503.3.peg.551; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; COG0784; LUCA.
DR   eggNOG; COG2198; LUCA.
DR   HOGENOM; HOG000272667; -.
DR   KO; K07648; -.
DR   OMA; AMLEQYI; -.
DR   OrthoDB; POG091H03T5; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.970; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR027460; ArcB_TM.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR014409; Sig_transdc_His_kin_hyb_ArcB.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PIRSF; PIRSF003182; ArcB; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47226; SSF47226; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; C5B762.
DR   SWISS-2DPAGE; C5B762.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR003182,
KW   ECO:0000256|SAAS:SAAS00049192};
KW   Cell inner membrane {ECO:0000256|PIRNR:PIRNR003182};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR003182};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Kinase {ECO:0000256|PIRNR:PIRNR003182, ECO:0000256|SAAS:SAAS00049154};
KW   Membrane {ECO:0000256|PIRNR:PIRNR003182, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR003182,
KW   ECO:0000256|SAAS:SAAS00049284};
KW   Phosphoprotein {ECO:0000256|PIRSR:PIRSR003182-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transcription {ECO:0000256|PIRNR:PIRNR003182};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR003182};
KW   Transferase {ECO:0000256|PIRNR:PIRNR003182,
KW   ECO:0000256|SAAS:SAAS00049232, ECO:0000313|EMBL:ACR67836.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|PIRNR:PIRNR003182}.
FT   TRANSMEM     20     46       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     58     77       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      153    223       PAS (PER-ARNT-SIM). {ECO:0000259|PROSITE:
FT                                PS50112}.
FT   DOMAIN      226    278       PAC (PAS-associated C-terminal).
FT                                {ECO:0000259|PROSITE:PS50113}.
FT   DOMAIN      289    507       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      527    643       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      678    771       HPt. {ECO:0000259|PROSITE:PS50894}.
FT   COILED       77    129       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     292    292       Phosphohistidine; by autocatalysis.
FT                                {ECO:0000256|PIRSR:PIRSR003182-50}.
FT   MOD_RES     576    576       4-aspartylphosphate. {ECO:0000256|PIRSR:
FT                                PIRSR003182-50, ECO:0000256|PROSITE-
FT                                ProRule:PRU00169}.
FT   MOD_RES     717    717       Phosphohistidine. {ECO:0000256|PIRSR:
FT                                PIRSR003182-50, ECO:0000256|PROSITE-
FT                                ProRule:PRU00110}.
SQ   SEQUENCE   778 AA;  87970 MW;  A6F6BC2D205D10E0 CRC64;
     MKQIRVLAQY YVDLMVKLGL VRFSILLASA LVLLAMVVQM AVTMLLRGQV DSIDVVRSVF
     FGLLITPWAV YFLSVVVEQL EESRQRLSKL VNKLEEMRHR DLKLNQQLKD NIRQLNQEIA
     DRVKAEEARL QVLDTLQHEI DQRELAQVEL EQQSALLRSF LDSSPDLVYY RNENGEFSGC
     NRAMELLTGK SEKQLIGLTP RDVYDQDIAQ KVIETDEKVF RHNVSLTYEQ WLVYPDGRKA
     CFELRKVPFY DRVGKRHGLM GFGRDITERK RYQDALENAS RDKTTFISTI SHELRTPLNG
     IVGLSRILLD TELNEEQLKY LKTIHVSAIA LGNIFNDIIE MDKLERRKVQ LDNQTIDFTG
     FLTDLENLSG LLVQPKGLSF TLAPDPALPH KVMVDGTRLR QILWNLIGNA VKFTQRGGVS
     VRVWREQQDK LLFEVRDTGI GIPPEEQDKI FAMYYQVKDM HGGKPATGTG IGLAVSKRLA
     QTMGGDIVVS SVAGEGACFT LSICAPVVEE TLSEPLAEEE MPLPALHVLL VEDIELNVIV
     ARSVLEKMGN SVDVAMSGTE ALAMFAPQEY DLVLLDIQLP DMTGLDIART LCRRYGKTAL
     PPLVALTANV LKDKKEYLDA GMDDVLSKPL AVPALTAVIH RFWDSTPLTV LEDGEPHAHD
     LCELLDTEML QQYLDLVGPQ LIEQSLAVFE RMMPGYLSVL ESNMTARDQK GITEEGHKIK
     GAAGSVGLRH LQQLAQQIQT PTLPAWWDNV QEWIDELKQE WRHDVQILRD WVVQTNKK
//

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