ID   A0A1V0PCQ4_LACLC        Unreviewed;       743 AA.
AC   A0A1V0PCQ4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   10-FEB-2021, entry version 24.
DE   RecName: Full=DD-transpeptidase {ECO:0000256|ARBA:ARBA00020219};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
DE   AltName: Full=Penicillin-insensitive transglycosylase {ECO:0000256|ARBA:ARBA00018834};
DE   AltName: Full=Penicillin-sensitive transpeptidase {ECO:0000256|ARBA:ARBA00022088};
DE   AltName: Full=Peptidoglycan TGase {ECO:0000256|ARBA:ARBA00013437};
GN   ORFNames=LLJM2_2186 {ECO:0000313|EMBL:ARE26923.1}, LLJM3_2396
GN   {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:UP000192003, ECO:0000313|Proteomes:UP000192161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JM2 {ECO:0000313|EMBL:ARE26923.1,
RC   ECO:0000313|Proteomes:UP000192003}, and JM3
RC   {ECO:0000313|EMBL:ARE24566.1, 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).
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:ARBA00000871};
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:ARBA00001517};
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DR   EMBL; CP015901; ARE24566.1; -; Genomic_DNA.
DR   EMBL; CP015900; ARE26923.1; -; Genomic_DNA.
DR   RefSeq; WP_011677170.1; NZ_WJUV01000018.1.
DR   Proteomes; UP000192003; Chromosome.
DR   Proteomes; UP000192161; 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   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:ARE24566.1};
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:ARBA00022679};
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"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..718
FT                   /note="Polar"
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
//