ID Q9CDV3_LACLA Unreviewed; 743 AA.
AC Q9CDV3;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp2A {ECO:0000313|EMBL:AAK06206.1};
GN ORFNames=L160485 {ECO:0000313|EMBL:AAK06206.1};
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK06206.1, ECO:0000313|Proteomes:UP000002196};
RN [1] {ECO:0000313|EMBL:AAK06206.1, ECO:0000313|Proteomes:UP000002196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403 {ECO:0000313|EMBL:AAK06206.1,
RC ECO:0000313|Proteomes:UP000002196};
RX PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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};
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DR EMBL; AE005176; AAK06206.1; -; Genomic_DNA.
DR PIR; D86888; D86888.
DR RefSeq; NP_268265.1; NC_002662.1.
DR RefSeq; WP_003129980.1; NC_002662.1.
DR AlphaFoldDB; Q9CDV3; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR PaxDb; 272623-L160485; -.
DR EnsemblBacteria; AAK06206; AAK06206; L160485.
DR GeneID; 69714287; -.
DR KEGG; lla:L160485; -.
DR PATRIC; fig|272623.7.peg.2267; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_2_9; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0016020; C: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; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 2A; 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.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
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 Reference proteome {ECO:0000313|Proteomes:UP000002196};
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 112..278
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 379..627
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..34
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 692..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 81975 MW; FBFD99982D67C560 CRC64;
MSENNNFSRR NKKESKKNSL KIPNLRPKKQ KKLEEEIEKP AKTKFGKFMK PIKRFWKRYN
LTKITIIFVL VAIVSTGSYL FYLAKTANVK VLQSSISAQT VIYDKDNNEA GNLYGQKGTP
VKIDQISKNI TNAVVATEDR TFYKNHGVNL KRFALAAVTL GRFGGGSTIT QQLAKNAYLT
QEQTIDRKAR EFFLALEINK HYSKDEILDM YLNNSYFGNG VWGIQDAALK YFGVPASEVT
VDEAASLAGM LKGPEIYNPL YEKGKYATDR RNTVLQNMVN AGYLEQSQAD TFMKVDLQAQ
LQDNYQSKSS QYKYPSYYNA VISEAERKYG LTLQEIMNNG YKIYTGMDQN MQSGLQKTYS
DPSFFPQASD GTYAQSASVA IDPKTGAVNA LVGNVNTEGS NSFTDYNYAT MSKRSPGSVI
KPLIVYAPAI EAGWSIDKTV DDSPADYNGW KPTDFDNQWR GQIPMYTALA NSYNIPAINT
YQAIGPKVGN ALGREFGLDL SSKNDVLPTA LGAGVETNPW QIAQAYQVFA NGGVMNDAHL
ITKIENAAGQ VVKTAKVTKK RVISKDTADK MTQMMLGTYT NGSAWKASPK SYTLAGKTGT
NEDQDQWVVG YTPDVVMALW VGYADGKYKL TGSSEGQTSV IFRQEASYML PYTKGTAFTV
ENPYAEAGVA AQEPYWTQQR QYQDDIVDQE QAEAHTTGNT PESSSSSSSS SSDSGGLDLG
KVGKDIGDAA KNAWDKVKGI FGN
//
