ID   A0A1V0PCQ4_LACLC        Unreviewed;       743 AA.
AC   A0A1V0PCQ4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   03-MAY-2023, entry version 33.
DE   SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:QSD64019.1};
GN   ORFNames=LL1196_2415 {ECO:0000313|EMBL:QSD64019.1};
OS   Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1359 {ECO:0000313|EMBL:QSD64019.1, ECO:0000313|Proteomes:UP000663552};
RN   [1] {ECO:0000313|EMBL:QSD64019.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1196 {ECO:0000313|EMBL:QSD64019.1};
RX   PubMed=32515029;
RA   Mahony J., Frantzen C., Vinogradov E., Sadovskaya I., Theodorou I.,
RA   Kelleher P., Chapot-Chartier M.P., Cambillau C., Holo H., van Sinderen D.;
RT   "The CWPS Rubik's cube: Linking diversity of cell wall polysaccharide
RT   structures with the encoded biosynthetic machinery of selected Lactococcus
RT   lactis strains.";
RL   Mol. Microbiol. 114:582-596(2020).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
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DR   EMBL; CP032148; QSD64019.1; -; Genomic_DNA.
DR   RefSeq; WP_011677170.1; NZ_WJUV01000018.1.
DR   EnsemblBacteria; ARE24566; ARE24566; LLJM3_2396.
DR   GeneID; 61110436; -.
DR   Proteomes; UP000663552; Chromosome.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 6.20.370.110; -; 1.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 1F; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   TIGRFAMs; TIGR02074; PBP_1a_fam; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:QSD64019.1};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          113..278
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          378..633
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   743 AA;  81995 MW;  E07146F32BB924A1 CRC64;
     MPENKNFSRR SKKETGKKSL KIPKIRPKKQ KKLEEEIEKP AKTKFGKFMR PIKRFWKRYN
     LTKITIIFVL VAIVATGSYL FYLAKTANVK VLQSSISAQT VIYDKDNNEA GNLYGQKGTP
     VKIDQISKNI TNAVVATEDR TFYENHGVNL KRFALAAVTL GRFGGGSTIT QQLAKNAYLT
     QEQTIDRKAR EFFLALEINK HYSKDEILDM YLNNSYFGNG VWGIQDAALK YFGVPASEVT
     VDEAASLAGM LKGPEIYNPL YEKGKYATDR RNTVLQNMVN AGYLEQSQAD SFMKVDLQAQ
     LQDNYQSKSS QYKYPSYYNA VISEAERKYG LTLQEIMNNG YKIYTGMDQN MQSGLQKTYA
     DPSFFPQAAD GTYAQSASVA IDPKTGAVNA LVGNVNTEGS NSFTDYNYAT MSKRSPGSVI
     KPLIVYAPAI EAGWSIDKTV DDSPADYNGW KPTDFDNQWR GQIPMYTALA NSYNIPAINT
     YQAIGPKVGN ALGREFGLDL NSKNDVLPTA LGAGVETNPW QIAQAYQAFA NGGVMNDAHL
     ITKIENAAGQ VVKTAKVNKK RVVSKDTADK MTQMMLGTYT NGSAWKASPK SYTLAGKTGT
     NEDQDQWVVG YTPDVVMALW VGYSDGKYKL TGSSEGQTSV IFRQEASYML PYTKGTPFTV
     ENPYAQAGVA AQQPYWTQQR QYQDDIVDQE QAEANTTGNT PESSSSSTSS SSDSNGLDLG
     KIGKNIGDAA KNAWDKVKGV FGN
//