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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //