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 04-NOV-2026, entry version 165. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_002695.2. DR RefSeq; WP_000809770.1; NZ_BLZJ01000050.1. DR AlphaFoldDB; P58363; -. DR BMRB; P58363; -. DR SMR; P58363; -. DR STRING; 155864.Z4574; -. 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; AACMHKI; -. DR BRENDA; 2.7.13.3; 2026. DR Proteomes; UP000000558; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009927; F:histidine phosphotransfer kinase activity; IEA:TreeGrafter. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; IEA:UniProtKB-ARBA. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1. DR CDD; cd00082; HisKA; 1. DR CDD; cd00088; HPT; 1. DR CDD; cd00130; PAS; 1. DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1. DR FunFam; 1.10.287.130:FF:000016; Aerobic respiration control sensor protein; 1. DR FunFam; 1.10.287.970:FF:000001; Aerobic respiration control sensor protein; 1. DR FunFam; 1.20.120.160:FF:000003; Aerobic respiration control sensor protein; 1. DR FunFam; 3.30.450.20:FF:000032; Aerobic respiration control sensor protein; 1. DR FunFam; 3.30.565.10:FF:000025; Aerobic respiration control sensor protein; 1. DR FunFam; 3.40.50.2300:FF:000107; Aerobic respiration control sensor protein; 1. DR Gene3D; 1.10.287.130; -; 1. DR Gene3D; 3.40.50.2300; -; 1. DR Gene3D; 1.10.287.970; His Kinase A (phosphoacceptor) domain; 1. DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1. DR Gene3D; 1.20.120.160; HPT domain; 1. DR Gene3D; 3.30.450.20; PAS domain; 1. DR InterPro; IPR027460; ArcB_TM_sf. DR InterPro; IPR011006; CheY-like_sf. DR InterPro; IPR036890; HATPase_C_sf. DR InterPro; IPR003594; HATPase_dom. DR InterPro; IPR005467; His_kinase_dom. DR InterPro; IPR003661; HisK_dim/P_dom. 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 NCBIfam; NF008302; arcB; 1. DR NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1. DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1. 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1. DR SUPFAM; SSF52172; CheY-like; 1. DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1. DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1. DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 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 //