ID   A0A1V0PCQ4_LACLC        Unreviewed;       743 AA.
AC   A0A1V0PCQ4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   30-AUG-2017, entry version 3.
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=.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).
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DR   EMBL; CP015901; ARE24566.1; -; Genomic_DNA.
DR   RefSeq; WP_011677170.1; NZ_LITF01000132.1.
DR   Proteomes; UP000192161; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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.
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; 2.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000313|EMBL:ARE24566.1};
KW   Transferase {ECO:0000256|SAAS:SAAS00705467};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     64     84       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      113    278       Transgly. {ECO:0000259|Pfam:PF00912}.
FT   DOMAIN      378    633       Transpeptidase. {ECO:0000259|Pfam:
FT                                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
//