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
//