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ARCB_ECO57
ID   ARCB_ECO57              Reviewed;         778 AA.
AC   P58363;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Aerobic respiration control sensor protein ArcB;
DE            EC=2.7.13.3;
GN   Name=arcB; OrderedLocusNames=Z4574, ECs4089;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Member of the two-component regulatory system ArcB/ArcA.
CC       Sensor-regulator protein for anaerobic repression of the arc modulon.
CC       Activates ArcA via a four-step phosphorelay. ArcB can also
CC       dephosphorylate ArcA by a reverse phosphorelay involving His-717 and
CC       Asp-576 (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- PTM: Activation requires a sequential transfer of a phosphate group
CC       from a His in the primary transmitter domain, to an Asp in the receiver
CC       domain and to a His in the secondary transmitter domain. {ECO:0000250}.
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DR   EMBL; AE005174; AAG58344.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37512.1; -; Genomic_DNA.
DR   PIR; A91140; A91140.
DR   PIR; D85985; D85985.
DR   RefSeq; NP_312116.1; NC_002695.1.
DR   RefSeq; WP_000809770.1; NZ_SEKU01000004.1.
DR   AlphaFoldDB; P58363; -.
DR   BMRB; P58363; -.
DR   SMR; P58363; -.
DR   STRING; 155864.EDL933_4438; -.
DR   EnsemblBacteria; AAG58344; AAG58344; Z4574.
DR   EnsemblBacteria; BAB37512; BAB37512; ECs_4089.
DR   GeneID; 916062; -.
DR   KEGG; ece:Z4574; -.
DR   KEGG; ecs:ECs_4089; -.
DR   PATRIC; fig|386585.9.peg.4268; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_114_15_6; -.
DR   OMA; VDWVIRL; -.
DR   BRENDA; 2.7.13.3; 2026.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0046777; P:protein autophosphorylation; IEA:UniProt.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00088; HPT; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.970; -; 1.
DR   Gene3D; 1.20.120.160; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR027460; ArcB_TM_sf.
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; IPR040642; HKR_ArcB_TM.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
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; PF18415; HKR_ArcB_TM; 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   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..778
FT                   /note="Aerobic respiration control sensor protein ArcB"
FT                   /id="PRO_0000074685"
FT   TOPO_DOM        1..25
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        47..57
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..778
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          153..223
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          226..278
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   DOMAIN          289..507
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   DOMAIN          527..643
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DOMAIN          678..771
FT                   /note="HPt"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT   MOD_RES         292
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         576
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         717
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   778 AA;  88010 MW;  C8AE004B007F9D30 CRC64;
     MKQIRLLAQY YVDLMMKLGL VRFSMLLALA LVVLAIVVQM AVTMVLHGQV ESIDVIRSIF
     FGLLITPWAV YFLSVVVEQL EESRQRLSRL VQKLEEMRER DLSLNVQLKD NIAQLNQEIA
     VREKAEAELQ ETFGQLKIEI KEREETQIQL EQQSSFLRSF LDASPDLVFY RNEDKEFSGC
     NRAMELLTGK SEKQLVHLKP ADVYSPEAAA KVIETDEKVF RHNVSLTYEQ WLDYPDGRKA
     CFEIRKVPYY DRVGKRHGLM GFGRDITERK RYQDALERAS RDKTTFISTI SHELRTPLNG
     IVGLSRILLD TELTAEQEKY LKTIHVSAVT LGNIFNDIID MDKMERRKVQ LDNQPVDFTS
     FLADLENLSA LQAQQKGLRF NLEPTLPLPH QVITDGTRLR QILWNLISNA VKFTQQGQVT
     VRVRYDEGDM LHFEVEDSGI GIPQDELDKI FAMYYQVKDS HGGKPATGTG IGLAVSRRLA
     KNMGGDITVT SEQGKGSTFT LTIHAPSVAE EVDDAFDEDD MPLPALNVLL VEDIELNVIV
     ARSVLEKLGN SVDVAMTGKA ALEMFKPGEY DLVLLDIQLP DMTGLDISRE LTKRYPREDL
     PPLVALTANV LKDKQEYLNA GMDDVLSKPL SVPALTAMIK KFWDTQDDEE STVTTEENSK
     SEALLDIPML EQYLELVGPK LITDGLAVFE KMMPGYVNVL ESNLTAQDKK GIVEEGHKIK
     GAAGSVGLRH LQQLGQQIQS PDLPAWEDNV GEWIEEMKEE WRHDVEVLKA WVAKATKK
 
 
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