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
//