ID A0A1V0PCQ4_LACLC Unreviewed; 743 AA. AC A0A1V0PCQ4; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 12-OCT-2022, entry version 30. DE SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:QSD64019.1}; DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:TEA96946.1}; GN ORFNames=BU174_10580 {ECO:0000313|EMBL:TEA96946.1}, LL1196_2415 GN {ECO:0000313|EMBL:QSD64019.1}; OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=1359 {ECO:0000313|EMBL:TEA96946.1, ECO:0000313|Proteomes:UP000298027}; RN [1] {ECO:0000313|EMBL:TEA96946.1, ECO:0000313|Proteomes:UP000298027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ASCC880900 {ECO:0000313|EMBL:TEA96946.1, RC ECO:0000313|Proteomes:UP000298027}; RA Ho C.H., Stanton-Cook M., Beatson S.A., Bansal N., Turner M.S.; RT "Draft Genome Sequence of Lactococcus lactis ASCC880900."; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {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 EMBL; MSGR01000162; TEA96946.1; -; Genomic_DNA. DR RefSeq; WP_011677170.1; NZ_WJUV01000018.1. DR EnsemblBacteria; ARE24566; ARE24566; LLJM3_2396. DR GeneID; 61110436; -. DR Proteomes; UP000298027; Unassembled WGS sequence. DR Proteomes; UP000663552; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; 1.10.3810.10; -; 1. DR Gene3D; 3.40.710.10; -; 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 Pfam; PF00912; Transgly; 1. DR Pfam; PF00905; Transpeptidase; 1. DR SUPFAM; SSF53955; SSF53955; 1. DR SUPFAM; SSF56601; SSF56601; 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 Membrane {ECO:0000256|SAM:Phobius}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Transferase {ECO:0000256|ARBA:ARBA00022676}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64..84 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 113..278 FT /note="Transgly" FT /evidence="ECO:0000259|Pfam:PF00912" FT DOMAIN 378..633 FT /note="Transpeptidase" FT /evidence="ECO:0000259|Pfam:PF00905" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 692..722 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..27 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 692..718 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //