ID C2GSR7_BIFLN Unreviewed; 727 AA.
AC C2GSR7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, 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=HMPREF0175_0063 {ECO:0000313|EMBL:EEI81596.1};
OS Bifidobacterium longum subsp. longum ATCC 55813.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=548480 {ECO:0000313|EMBL:EEI81596.1, ECO:0000313|Proteomes:UP000004443};
RN [1] {ECO:0000313|EMBL:EEI81596.1, ECO:0000313|Proteomes:UP000004443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55813 {ECO:0000313|EMBL:EEI81596.1,
RC ECO:0000313|Proteomes:UP000004443};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEI81596.1}.
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DR EMBL; ACHI01000005; EEI81596.1; -; Genomic_DNA.
DR AlphaFoldDB; C2GSR7; -.
DR HOGENOM; CLU_006354_6_2_11; -.
DR Proteomes; UP000004443; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; 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: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 PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF34; PENICILLIN-BINDING PROTEIN 1A; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 52..223
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 315..556
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 603..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 727 AA; 77788 MW; 660DCF303152D0D2 CRC64;
MLGIFFSLIG LGLLAGIAVF AYLYTTTEVP QPEKFALAEK TTVYYADGTT AIGSYAEQNR
EIISCEGLPD YIGNAIVASE NRTFYTDKGL DLKGIARAFI NNVTKGTRQG GSTITQQYAE
RYYMGETTSY VGKAREAIMA IKIAQTESKD EVLCNYMNTI YLGRNSYGIQ AAAKAYFNKD
AKDLTLSEAA MIAGIIPSPS TWDPADNADM AKSRFKRVLN IMQEDGYITA KQHTDAKFPQ
TAAVAQQNEY AGPNGYLLDM VRRELVQSKA FTKEDLDTGG YKIITTIDKS KQDLMQSIGD
TRLDDMPESL QIGGIALDPK TGEVLSVYAG SDYLSKQLNN ADQAVFEPGS TMKPFALLGA
AQSGVSFDTL FNGNSHQHFT GLDQEVNNAL ENNWGNINLY QATANSVNTV FMNVNEHLTP
KRTAAIAHEA GIQGDIDENS MYNVLGINAL TVWDLAQGHS TIANNGVKNT LHMVSKVLDS
NNKDMYNAPS NGTKVFDAND CALVQKAMQG TTTYGTAAGT SSMLGRPVAG KSGTANDEMA
SSFVGYTPSM MNVWAIWNPD DKGNPQVVPA FSGYGVSSTG YPAHLFQEFM AQALQGTEAE
QFPTAKDNGK IGGSDGTWGL GKGQSSGLSN NTNKQSTEDT QKQAEQDAQQ KAAEEEAKKQ
QQAQEFAQQC LANPSYSTEC PNYPGTTTGG DGNAGNNTGG DNGNNTGNDN GNSGGTGGNT
GTNGVTQ
//
