BLAR_BACLI
ID BLAR_BACLI Reviewed; 601 AA.
AC P12287;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Regulatory protein BlaR1;
GN Name=blaR1; Synonyms=penR1;
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=3040663; DOI=10.1128/jb.169.9.3873-3878.1987;
RA Kobayashi T., Zhu Y.F., Nicholls N.J., Lampen J.O.;
RT "A second regulatory gene, blaR1, encoding a potential penicillin-binding
RT protein required for induction of beta-lactamase in Bacillus
RT licheniformis.";
RL J. Bacteriol. 169:3873-3878(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-74.
RC STRAIN=ATCC 25972 / DSM 8782 / NCIMB 11109 / IMET 10723 / 749/C;
RX PubMed=3260234; DOI=10.1128/jb.170.7.3206-3212.1988;
RA Wittman V., Wong H.C.;
RT "Regulation of the penicillinase genes of Bacillus licheniformis:
RT interaction of the pen repressor with its operators.";
RL J. Bacteriol. 170:3206-3212(1988).
RN [3]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2404938; DOI=10.1128/jb.172.2.1137-1141.1990;
RA Zhu Y.F., Curran I.H.A., Joris B., Ghuysen J.-M., Lampen J.O.;
RT "Identification of BlaR, the signal transducer for beta-lactamase
RT production in Bacillus licheniformis, as a penicillin-binding protein with
RT strong homology to the OXA-2 beta-lactamase (class D) of Salmonella
RT typhimurium.";
RL J. Bacteriol. 172:1137-1141(1990).
RN [4]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=9076730; DOI=10.1046/j.1365-2958.1997.2761642.x;
RA Hardt K., Joris B., Lepage S., Brasseur R., Lampen J.O., Frere J.M.,
RA Fink A.L., Ghuysen J.M.;
RT "The penicillin sensory transducer, BlaR, involved in the inducibility of
RT beta-lactamase synthesis in Bacillus licheniformis is embedded in the
RT plasma membrane via a four-alpha-helix bundle.";
RL Mol. Microbiol. 23:935-944(1997).
RN [5] {ECO:0007744|PDB:1NRF}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 346-601, AND DOMAIN.
RX PubMed=14596597; DOI=10.1021/bi034976a;
RA Kerff F., Charlier P., Colombo M.L., Sauvage E., Brans A., Frere J.M.,
RA Joris B., Fonze E.;
RT "Crystal structure of the sensor domain of the BlaR penicillin receptor
RT from Bacillus licheniformis.";
RL Biochemistry 42:12835-12843(2003).
CC -!- FUNCTION: Integral membrane protein involved in sensing of the presence
CC of beta-lactam antibiotics and transduction of the information to the
CC cytoplasm. Mechanistically, activation of the signal transducer
CC involves acylation of a serine in the C-terminal sensor domain upon
CC binding of the beta-lactam antibiotic. In turn, a conformational change
CC occurs and the signal is transmitted from the cell surface to the
CC cytoplasm. There, the zinc protease domain is activated and initiates
CC autoproteolysis as well as cleavage of the transcriptional repressor
CC BlaI leading to derepression of antibiotic resistance genes.
CC {ECO:0000250|UniProtKB:P18357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9076730};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9076730}.
CC -!- PTM: Carboxylation occurs on two lysine residues. Carboxylation at
CC 'Lys-405' activates the active site serine residue for acylation. On
CC acylation, the lysine side chain experiences a spontaneous
CC decarboxylation that entraps the sensor in its activated state.
CC {ECO:0000250|UniProtKB:P18357}.
CC -!- SIMILARITY: Belongs to the peptidase M56 family. {ECO:0000305}.
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DR EMBL; M17368; AAA22273.1; -; Genomic_DNA.
DR EMBL; M21337; AAA22651.1; -; Genomic_DNA.
DR PIR; I39790; I39790.
DR PDB; 1NRF; X-ray; 2.50 A; A=346-601.
DR PDBsum; 1NRF; -.
DR AlphaFoldDB; P12287; -.
DR SMR; P12287; -.
DR ChEMBL; CHEMBL1744487; -.
DR MEROPS; M56.003; -.
DR EvolutionaryTrace; P12287; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR InterPro; IPR008756; Peptidase_M56.
DR Pfam; PF05569; Peptidase_M56; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..601
FT /note="Regulatory protein BlaR1"
FT /id="PRO_0000195469"
FT TOPO_DOM 1..8
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TRANSMEM 9..26
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TOPO_DOM 27..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TRANSMEM 36..52
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TOPO_DOM 53..115
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TRANSMEM 116..133
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TOPO_DOM 134..322
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TRANSMEM 323..339
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:9076730"
FT TOPO_DOM 340..601
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:9076730"
FT REGION 354..601
FT /note="Beta-lactam antibiotic sensor domain"
FT /evidence="ECO:0000305|PubMed:14596597"
FT ACT_SITE 402
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P18357"
FT MOD_RES 405
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:P18357"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:1NRF"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 372..380
FT /evidence="ECO:0007829|PDB:1NRF"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 391..395
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 405..414
FT /evidence="ECO:0007829|PDB:1NRF"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 443..449
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 452..462
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 464..473
FT /evidence="ECO:0007829|PDB:1NRF"
FT TURN 484..489
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 497..508
FT /evidence="ECO:0007829|PDB:1NRF"
FT TURN 509..512
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 516..526
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 527..531
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 534..544
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 550..559
FT /evidence="ECO:0007829|PDB:1NRF"
FT STRAND 564..574
FT /evidence="ECO:0007829|PDB:1NRF"
FT HELIX 578..592
FT /evidence="ECO:0007829|PDB:1NRF"
SQ SEQUENCE 601 AA; 68417 MW; 84677A8DA448518E CRC64;
MSSSFFIPFL VSQILLSLFF SIIILIKKLL RTQITVGTHY YISVISLLAL IAPFIPFHFL
KSHHFDWILN LGGAQSALSQ THSTDKTTEA IGQHVNWVQD FSLSIEQSSS KMIDSAFFAV
WILGVAVMLL ATLYSNLKIG KIKKNLQIVN NKELLSLFHT CKEEIRFHQK VILSRSPLIK
SPITFGVIRP YIILPKDISM FSADEMKCVL LHELYHCKRK DMLINYFLCL LKIVYWFNPL
VWYLSKEAKT EMEISCDFAV LKTLDKKLHL KYGEVILKFT SIKQRTSSLL AASEFSSSYK
HIKRRIVTVV NFQTASPLLK AKSALVFTLV LGAILAGTPS VSILAMQKET RFLPGTNVEY
EDYSTFFDKF SASGGFVLFN SNRKKYTIYN RKESTSRFAP ASTYKVFSAL LALESGIITK
NDSHMTWDGT QYPYKEWNQD QDLFSAMSSS TTWYFQKLDR QIGEDHLRHY LKSIHYGNED
FSVPADYWLD GSLQISPLEQ VNILKKFYDN EFDFKQSNIE TVKDSIRLEE SNGRVLSGKT
GTSVINGELH AGWFIGYVET ADNTFFFAVH IQGEKRAAGS SAAEIALSIL DKKGIYPSVS
R
