ID ARCB_ECOLI Reviewed; 778 AA. AC P0AEC3; P22763; Q2M902; DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 27-MAR-2024, entry version 156. DE RecName: Full=Aerobic respiration control sensor protein ArcB; DE EC=2.7.13.3; GN Name=arcB; OrderedLocusNames=b3210, JW5536; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=2201868; DOI=10.1111/j.1365-2958.1990.tb00642.x; RA Iuchi S., Matsuda Z., Fujiwara T., Lin E.C.C.; RT "The arcB gene of Escherichia coli encodes a sensor-regulator protein for RT anaerobic repression of the arc modulon."; RL Mol. Microbiol. 4:715-727(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP SEQUENCE REVISION TO 469-470. RX PubMed=16397293; DOI=10.1093/nar/gkj405; RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., RA Thomson N.R., Wishart D., Wanner B.L.; RT "Escherichia coli K-12: a cooperatively developed annotation snapshot RT -- 2005."; RL Nucleic Acids Res. 34:1-9(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP CHARACTERIZATION. RC STRAIN=M15; RX PubMed=9286997; DOI=10.1128/jb.179.17.5429-5435.1997; RA Georgellis D., Lynch A.S., Lin E.C.C.; RT "In vitro phosphorylation study of the arc two-component signal RT transduction system of Escherichia coli."; RL J. Bacteriol. 179:5429-5435(1997). RN [6] RP CHARACTERIZATION. RC STRAIN=M15; RX PubMed=9830034; DOI=10.1074/jbc.273.49.32864; RA Georgellis D., Kwon O., De Wulf P., Lin E.C.C.; RT "Signal decay through a reverse phosphorelay in the arc two-component RT signal transduction system."; RL J. Biol. Chem. 273:32864-32869(1998). RN [7] RP PHOSPHORYLATION AT HIS-292 AND HIS-717, AND MUTAGENESIS OF HIS-292; ASP-576 RP AND HIS-717. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=10851007; DOI=10.1128/jb.182.13.3858-3862.2000; RA Kwon O., Georgellis D., Lin E.C.C.; RT "Phosphorelay as the sole physiological route of signal transmission by the RT arc two-component system of Escherichia coli."; RL J. Bacteriol. 182:3858-3862(2000). RN [8] RP SUBCELLULAR LOCATION. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 660-778. RX PubMed=9054511; DOI=10.1016/s0092-8674(00)81914-5; RA Kato M., Mizuno T., Shimizu T., Hakoshima T.; RT "Insights into multistep phosphorelay from the crystal structure of the C- RT terminal HPt domain of ArcB."; RL Cell 88:717-723(1997). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 659-776 IN COMPLEX WITH CHEY. RX PubMed=9761838; DOI=10.1107/s0907444997007075; RA Kato M., Mizuno T., Hakoshima T.; RT "Crystallization of a complex between a novel C-terminal transmitter, HPt RT domain, of the anaerobic sensor kinase ArcB and the chemotaxis response RT regulator CheY."; RL Acta Crystallogr. D 54:140-142(1998). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 659-776. RX PubMed=10531481; DOI=10.1107/s0907444999010392; RA Kato M., Mizuno T., Shimizu T., Hakoshima T.; RT "Refined structure of the histidine-containing-phosphotransfer (HPt) domain RT of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57-A RT resolution."; RL Acta Crystallogr. D 55:1842-1849(1999). 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. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L- CC histidine.; EC=2.7.13.3; CC -!- INTERACTION: CC P0AEC3; P0AFN2: pspC; NbExp=3; IntAct=EBI-557109, EBI-1134561; CC -!- SUBCELLULAR LOCATION: Cell inner membrane CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein CC {ECO:0000269|PubMed:15919996}. 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. 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; X53315; CAA37397.1; -; Genomic_DNA. DR EMBL; U18997; AAA58012.1; -; Genomic_DNA. DR EMBL; U00096; AAT48172.1; -; Genomic_DNA. DR EMBL; AP009048; BAE77254.1; -; Genomic_DNA. DR PIR; D65112; RGECAR. DR RefSeq; WP_000809774.1; NZ_STEB01000012.1. DR RefSeq; YP_026207.1; NC_000913.3. DR PDB; 1A0B; X-ray; 2.06 A; A=654-778. DR PDB; 1BDJ; X-ray; 2.68 A; B=654-778. DR PDB; 1FR0; NMR; -; A=654-778. DR PDB; 2A0B; X-ray; 1.57 A; A=654-778. DR PDB; 2KSD; NMR; -; A=1-115. DR PDBsum; 1A0B; -. DR PDBsum; 1BDJ; -. DR PDBsum; 1FR0; -. DR PDBsum; 2A0B; -. DR PDBsum; 2KSD; -. DR AlphaFoldDB; P0AEC3; -. DR BMRB; P0AEC3; -. DR SMR; P0AEC3; -. DR BioGRID; 4263422; 413. DR BioGRID; 852196; 2. DR DIP; DIP-47915N; -. DR IntAct; P0AEC3; 7. DR MINT; P0AEC3; -. DR STRING; 511145.b3210; -. DR iPTMnet; P0AEC3; -. DR jPOST; P0AEC3; -. DR PaxDb; 511145-b3210; -. DR EnsemblBacteria; AAT48172; AAT48172; b3210. DR GeneID; 75206066; -. DR GeneID; 947887; -. DR KEGG; ecj:JW5536; -. DR KEGG; eco:b3210; -. DR PATRIC; fig|1411691.4.peg.3519; -. DR EchoBASE; EB0060; -. DR eggNOG; COG0784; Bacteria. DR eggNOG; COG2198; Bacteria. DR eggNOG; COG5002; Bacteria. DR HOGENOM; CLU_000445_114_15_6; -. DR InParanoid; P0AEC3; -. DR OMA; AMLEQYI; -. DR OrthoDB; 9770795at2; -. DR PhylomeDB; P0AEC3; -. DR BioCyc; EcoCyc:ARCB-MONOMER; -. DR BioCyc; MetaCyc:ARCB-MONOMER; -. DR BRENDA; 2.7.13.3; 2026. DR EvolutionaryTrace; P0AEC3; -. DR PRO; PR:P0AEC3; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; NAS:EcoCyc. DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc. DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc. DR GO; GO:0046777; P:protein autophosphorylation; IMP:CACAO. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro. DR GO; GO:0070482; P:response to oxygen levels; IDA:EcoCyc. DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc. 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 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_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 NCBIfam; TIGR00229; sensory_box; 1. DR PANTHER; PTHR43719:SF27; AEROBIC RESPIRATION CONTROL SENSOR PROTEIN ARCB; 1. DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase; KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; KW Transcription; Transcription regulation; Transferase; Transmembrane; KW Transmembrane helix; Two-component regulatory system. FT CHAIN 1..778 FT /note="Aerobic respiration control sensor protein ArcB" FT /id="PRO_0000074684" 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 ECO:0000269|PubMed:10851007" FT MOD_RES 576 FT /note="4-aspartylphosphate" FT /evidence="ECO:0000305" FT MOD_RES 717 FT /note="Phosphohistidine" FT /evidence="ECO:0000305|PubMed:10851007" FT MUTAGEN 292 FT /note="H->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:10851007" FT MUTAGEN 576 FT /note="D->A: Loss of activity." FT /evidence="ECO:0000269|PubMed:10851007" FT MUTAGEN 717 FT /note="H->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:10851007" FT CONFLICT 469..470 FT /note="Missing (in Ref. 2; AAA58012)" FT /evidence="ECO:0000305" FT HELIX 27..45 FT /evidence="ECO:0007829|PDB:2KSD" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:2KSD" FT TURN 58..60 FT /evidence="ECO:0007829|PDB:2KSD" FT HELIX 61..78 FT /evidence="ECO:0007829|PDB:2KSD" FT HELIX 660..664 FT /evidence="ECO:0007829|PDB:2A0B" FT HELIX 667..676 FT /evidence="ECO:0007829|PDB:2A0B" FT HELIX 679..705 FT /evidence="ECO:0007829|PDB:2A0B" FT HELIX 709..725 FT /evidence="ECO:0007829|PDB:2A0B" FT HELIX 729..738 FT /evidence="ECO:0007829|PDB:2A0B" FT HELIX 746..775 FT /evidence="ECO:0007829|PDB:2A0B" SQ SEQUENCE 778 AA; 87983 MW; DD61EA6ECF95AD30 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 KMMPGYVSVL ESNLTAQDKK GIVEEGHKIK GAAGSVGLRH LQQLGQQIQS PDLPAWEDNV GEWIEEMKEE WRHDVEVLKA WVAKATKK //