ARCB_ECOLI
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 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=b3210, JW5536;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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.
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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; P0AEC3; -.
DR PRIDE; P0AEC3; -.
DR EnsemblBacteria; AAT48172; AAT48172; b3210.
DR EnsemblBacteria; BAE77254; BAE77254; BAE77254.
DR GeneID; 66672888; -.
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; VDWVIRL; -.
DR PhylomeDB; P0AEC3; -.
DR BioCyc; EcoCyc:ARCB-MON; -.
DR BioCyc; MetaCyc:ARCB-MON; -.
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:0005887; C:integral component of plasma membrane; ISM: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:0018106; P:peptidyl-histidine phosphorylation; IMP:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0070482; P:response to oxygen levels; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
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 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
