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Database: UniProt
Entry: A0A157SGE2_9BORD
LinkDB: A0A157SGE2_9BORD
Original site: A0A157SGE2_9BORD 
ID   A0A157SGE2_9BORD        Unreviewed;      1395 AA.
AC   A0A157SGE2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Two-component hybrid sensor and regulator {ECO:0000313|EMBL:SAI69414.1};
DE            EC=2.7.13.3 {ECO:0000313|EMBL:SAI69414.1};
DE            EC=2.7.3.- {ECO:0000313|EMBL:SAI69414.1};
GN   Name=arcB {ECO:0000313|EMBL:SAI69414.1};
GN   ORFNames=SAMEA3906486_02480 {ECO:0000313|EMBL:SAI69414.1};
OS   Bordetella ansorpii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=288768 {ECO:0000313|EMBL:SAI69414.1, ECO:0000313|Proteomes:UP000076848};
RN   [1] {ECO:0000313|EMBL:SAI69414.1, ECO:0000313|Proteomes:UP000076848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H050680373 {ECO:0000313|EMBL:SAI69414.1,
RC   ECO:0000313|Proteomes:UP000076848};
RG   Pathogen Informatics;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC         glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC         ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:82795; EC=2.1.1.80;
CC         Evidence={ECO:0000256|ARBA:ARBA00001541};
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DR   EMBL; FKIF01000006; SAI69414.1; -; Genomic_DNA.
DR   STRING; 288768.SAMEA3906486_02480; -.
DR   Proteomes; UP000076848; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd16434; CheB-CheR_fusion; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17580; REC_2_DhkD-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR035909; CheB_C.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR036804; CheR_N_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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR24422:SF25; CONSERVED HYPOTHETICAL CHEMOTAXIS PROTEIN; 1.
DR   Pfam; PF01339; CheB_methylest; 1.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF13596; PAS_10; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00138; MeTrc; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 3.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS50122; CHEB; 1.
DR   PROSITE; PS50123; CHER; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|PROSITE-
KW   ProRule:PRU00050}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076848};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SAI69414.1}.
FT   DOMAIN          37..216
FT                   /note="CheB-type methylesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50122"
FT   DOMAIN          243..496
FT                   /note="CheR-type methyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50123"
FT   DOMAIN          837..887
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          888..961
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          963..1013
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1031..1253
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1275..1392
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          680..774
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT   MOD_RES         1325
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1395 AA;  154386 MW;  E02115A5AF55697B CRC64;
     MAPWQAHRDK DNRMTPDMPD SGPPPDNQKH LMTSDLTFPV VGIGASAGGI EALKVFFENM
     PPKPDMAFVV VLHLSPKHDS VAHHILQAVT DLPIVQVTHT MPVQKNHVYV IPPAAGLQMN
     DGYLRLKAHE RPMGQPIAID VFFRALADVH KSKSIGIILT GGGSDGSVGL ARIKEQGGIT
     IAQQPGDAQH DAMPRNAIAT GMVDIILPVA QMPARLKGIR ENMARIHMPA PVGDPLDPDS
     PEHAHEESPA ERKSLLDILT LLRTRTGHDF RHYKKATVLR RIERRMQVTG VPDMQSYAAM
     LHETAEETPK LLGDMLIGVT QFFRDKEAYE ALEQQAIGPL VNGRDGTPPP SVRVWTAGCA
     TGEEAYSMAM LLSSYAEKQP SPPRLQVFAT DIDEPSLATG RAGLYPAAID TDVSPGMLQS
     YFTKDEAGYR IKKEIRERVL FAPHNVLRDP PFSKLDLVTC RNLLIYLDRE VQMDVLRMFH
     FALKPGGFLF LGSSESADAC ENLFTVVDKR NRLYQAKGAA YVHRTIPTLP SATFDKVIRA
     VPAESSPSRR GKTSFAEIHQ RALEQYAPPS VIVDHEANIV HMSDRAGRFL RHAGGEPSRN
     LPALVQPELR MELRTAMFQA LHSRKSVEAR RVEMTVGERR MYVNMVVRPF RHEESGNDFM
     LVIFDEVEAI MGEDGEAQAG KVATSMLAQL EAELQQAKDR LQLTMEQSET STEELKASNE
     ELQAINEELR SATEELETGK EELQSVNEEL VTVNSELKSK VEETAKINDD LQNLIASTDI
     ATVFVDRGMR IKWFTPRATD IFSVIASDAG RSLLDITHRL NYPDLARDAG SVFDSLRTVE
     REISGSNGRW YLARLLPYRS AEHRIEGAVL TFIDITDRCE AEERLRLGEA HMRLMAQSTK
     DFAIITIDQN GCIATWNSGA HIIFGYREEE AVGQPLGIIF TREDVENGEP QKEMERARTR
     GYASDERWLR RKDGSRIFCT GSINPMRDDH FDGYAKIARD VTEQRRKESE QENRLESSRD
     DSRLKDEFFA IMSHELKHPL NLIQLNADLL ARTPAVRGSP STARAAETIQ HSVRSQARII
     EDLLDMARVQ TGKLKLNRGV VSLTDTVESI LSVLRHTAAS ADVDLRSDYD AADALHIDAD
     STRVEQIIWN LLNNGIKFTP VGGSVSVSLS RDGQMARLDV IDTGEGIEPA FLAKVFDMFS
     QADMRHRGIN RDGLGIGLGV VGQLVQAHGG NIEAYSEGKG RGARFSVWLP LAQPAHADAD
     HVPAPPMDGQ LTGLRILIVD DSEDILDTFQ ALLEMEGAQV AIANSGARAL ETLDASTAYD
     LIISDIGMPN MDGYQFMAEV RNRFPDLKIP AIALTGYGSK DHIDKAAQAG FTTHLNKPIP
     LDALVEAVSH ALGRS
//
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