ID A0A1V0PCQ4_LACLC Unreviewed; 743 AA. AC A0A1V0PCQ4; DT 07-JUN-2017, integrated into UniProtKB/TrEMBL. DT 07-JUN-2017, sequence version 1. DT 31-JUL-2019, entry version 15. DE SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:ARE24566.1}; GN ORFNames=LLJM3_2396 {ECO:0000313|EMBL:ARE24566.1}; OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; OC Lactococcus. OX NCBI_TaxID=1359 {ECO:0000313|EMBL:ARE24566.1, ECO:0000313|Proteomes:UP000192161}; RN [1] {ECO:0000313|EMBL:ARE24566.1, ECO:0000313|Proteomes:UP000192161} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JM3 {ECO:0000313|EMBL:ARE24566.1, RC ECO:0000313|Proteomes:UP000192161}; RX PubMed=28356072; DOI=10.1186/s12864-017-3650-5; RA Kelleher P., Bottacini F., Mahony J., Kilcawley K.N., van Sinderen D.; RT "Comparative and functional genomics of the Lactococcus lactis taxon; RT insights into evolution and niche adaptation."; RL BMC Genomics 18:267-267(2017). 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; CP015901; ARE24566.1; -; Genomic_DNA. DR RefSeq; WP_011677170.1; NZ_MUHT01000101.1. DR BioCyc; GCF_002078935:LLJM3_RS12315-MONOMER; -. DR Proteomes; UP000192161; Chromosome. DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0008658; F:penicillin binding; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.3810.10; -; 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:0000313|EMBL:ARE24566.1}; KW Complete proteome {ECO:0000313|Proteomes:UP000192161}; KW Hydrolase {ECO:0000313|EMBL:ARE24566.1}; KW Protease {ECO:0000313|EMBL:ARE24566.1}; KW Transferase {ECO:0000256|SAAS:SAAS01077424}. FT REGION 1 33 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 692 722 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 11 27 Basic. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 692 718 Polar. {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 //