ID   Q9LBL1_BACCE            Unreviewed;       662 AA.
AC   Q9LBL1;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000256|ARBA:ARBA00012448};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   Name=pbp3 {ECO:0000313|EMBL:BAA95415.1};
OS   Bacillus cereus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396 {ECO:0000313|EMBL:BAA95415.1};
RN   [1] {ECO:0000313|EMBL:BAA95415.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ts-4 {ECO:0000313|EMBL:BAA95415.1};
RX   PubMed=11866118; DOI=10.1271/bbb.66.44;
RA   Miyamoto T., Sayed M.A., Sasahara R., Sukimoto K., Umezaki A., Honjoh K.,
RA   Iio M., Hatano S.;
RT   "Cloning and overexpression of Bacillus cereus penicillin-binding protein 3
RT   gene in Escherichia coli.";
RL   Biosci. Biotechnol. Biochem. 66:44-50(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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DR   EMBL; AB039287; BAA95415.1; -; Genomic_DNA.
DR   PIR; JC7803; JC7803.
DR   AlphaFoldDB; Q9LBL1; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR007887; MecA_N.
DR   InterPro; IPR032710; NTF2-like_dom_sf.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   Pfam; PF05223; MecA_N; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF54427; NTF2-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT   DOMAIN          24..142
FT                   /note="NTF2-like N-terminal transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF05223"
FT   DOMAIN          150..317
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          351..659
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          144..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   662 AA;  73066 MW;  66589F36B810CDFB CRC64;
     MRKIWGILSL CLTFMLVGCG KEEKPQEAFD TYVKAWNKQK FADMYDQLSK NAKKDISKKE
     FTEKYEKIYS GIEVKDLKVE TGEVKEDKKD EGPVPFKVSM DTVGGKITFG HEAKMVKEKD
     GDKESWKIDW TPDFIFPGMT KDSKVRMQTT QPKRGEIYDR NGKGSCTNGK ASEIGLIPEK
     LGDAAPQTKE TVAKLLNMSV EEIDQKLAAK WVKPGYLVPI GILPEGATQN TYIDLPGVST
     KPVNVRTYPL GEAAAHLTGY IGKVNAEDLK TLQKKGYQAD DPVGKAGLEQ VLEEKLRGKK
     GDRVFVEDAQ GKEIKNLAKT DAVDGENVTL TIDSAVQGKP YNEMKGEAGS SAAINPKSGE
     TIALVSSPAY DPNIIARGTS KAQREAWNND PKKPMTNRFT QLSVPGSVFK PITAAIGLET
     KTIDPKEELK IEGLKWTKDS SWGNYYVTRC ERCKFRLILD KAMKYSDNIY FAQEALKIGK
     DKFMSEAKKF GFDEKLPIEY GFPASKIAND GIKNDIQMAD TGYGQGQVLM TPLHLALTYA
     PIVNDGTIPS PYIIKTDKQP KAWKENVISK GNQDILKTAM TKVINDPDGT GKIAKIDGMT
     LAGKTGTAEL RVSKEAEGKE LGRFAAFDLN SPDMVITMMI DDVKGRGGSN IPAEKVKHVF
     QK
//