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Database: UniProt
Entry: E3R3J5_9LACO
LinkDB: E3R3J5_9LACO
Original site: E3R3J5_9LACO 
ID   E3R3J5_9LACO            Unreviewed;       770 AA.
AC   E3R3J5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=LBKG_00866 {ECO:0000313|EMBL:EFQ44984.1};
OS   Lactobacillus crispatus CTV-05.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=440496 {ECO:0000313|EMBL:EFQ44984.1, ECO:0000313|Proteomes:UP000005124};
RN   [1] {ECO:0000313|EMBL:EFQ44984.1, ECO:0000313|Proteomes:UP000005124}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTV-05 {ECO:0000313|EMBL:EFQ44984.1,
RC   ECO:0000313|Proteomes:UP000005124};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease.;
RA   Ward D., Xu Q., Earl A., Liu Y., Feldgarden M., Gevers D., Young S.K.,
RA   Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D., Howarth C., Jen D., Larson L., Mehta T.,
RA   Neiman D., Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Lactobacillus crispatus strain CTV-05.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
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; GL531737; EFQ44984.1; -; Genomic_DNA.
DR   RefSeq; WP_005719682.1; NZ_GL531737.1.
DR   AlphaFoldDB; E3R3J5; -.
DR   HOGENOM; CLU_006354_2_5_9; -.
DR   Proteomes; UP000005124; Unassembled WGS sequence.
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; 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:SF29; PENICILLIN-BINDING PROTEIN 1A/1B; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          78..255
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          349..629
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..753
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..770
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   770 AA;  85238 MW;  BA079A290CB6DBC9 CRC64;
     MADNNNNMKR ESRRDYHGRR PSSGHLWIRI IKWIFLLIFL IVISGIGLFA FYAKDAPNIS
     QDQLQSGKSS SLYTNNGKFL LSLGSEKRIY VKNKDIPQQL KDAVVSVEDK RFYKDKLGVD
     PIRIIGSMLT NAKSNSIAAG GSTITQQLVK LTVFSTAASQ RTLKRKAQEA WLAMKVQHEF
     SKDQILEFYI NKVFMNYGNY GMGTASNYYY GKPLSKLDLA QTALIAGMPN APVAYDPYLY
     PQKAKYRRDI VLKTMLQNDK ITKAEYNQAV AEPISKGLKS HRNNNESKIR KIDDPYIKEV
     ISEVKSKGFD PYHDNLKITI NIDQKAQNKL YELANNGSVP FTNNKMQIGA TVVDPNNGHV
     VAILGGRHLP SVQLGLDRAV QTGRSTGSSI KPVLDYAPAI QYLNWSTAKM IDDSKYVYPG
     TNIQLYDWDN KYDGMMTMRH ALEQSRNVPA VKTLAEVGVK RASAFARRMG VNVSSKSGLS
     VAIGANASSL QMTGAYSAFA TMGVYHKPQF VSKIETPDGL TRNYDSNGVR VMKKSTAYMI
     TDMLKGVIKR GSGTNAKIAD LYQAGKTGTV KYSDEDLAKY PSYNSTPKDS WFVGYTRSYV
     MGVWTGYDNL KDGTISGIGQ QSAQLMYKSM MTYLMNNKPN LDWKQPSSVV RAKIVNNSNP
     PELATSGGTW QLFVRGHAPA GIGNSAASYD EDDEETDTSS DNTGTTPSSS RTAVTQSSSS
     RENGSSSQSN SSQRASSSQR KTQSSSTQQS SSTRKPEEES HERNDDSDND
//
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