ID A0A364V4B0_9CORY Unreviewed; 454 AA.
AC A0A364V4B0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Fragment;
GN ORFNames=DLJ54_08230 {ECO:0000313|EMBL:RAV31458.1};
OS Corynebacterium heidelbergense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=2055947 {ECO:0000313|EMBL:RAV31458.1, ECO:0000313|Proteomes:UP000251577};
RN [1] {ECO:0000313|EMBL:RAV31458.1, ECO:0000313|Proteomes:UP000251577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=647 {ECO:0000313|EMBL:RAV31458.1,
RC ECO:0000313|Proteomes:UP000251577};
RX PubMed=29958724;
RA Braun M.S., Wang E., Zimmermann S., Wink M.;
RT "Corynebacterium heidelbergense sp. nov., isolated from the preen glands of
RT Egyptian geese (Alopochen aegyptiacus).";
RL Syst. Appl. Microbiol. 0:0-0(2018).
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:RAV31458.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QHCV01000092; RAV31458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364V4B0; -.
DR Proteomes; UP000251577; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000251577}.
FT DOMAIN 44..217
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 309..427
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 454
FT /evidence="ECO:0000313|EMBL:RAV31458.1"
SQ SEQUENCE 454 AA; 48338 MW; 0B2FB0E3A383335B CRC64;
MAVMIIVPIV AFFAAYAVTR VPEPEELVNN QISYILASDN QTELARIVPP EGNRQNVKIE
EIPKPVRDAV LAAEDRNFYD NPGFSITGFG RAALGQVFGK SGAGGGSTIT QQYVKNALVG
DDFSLVRKAK ELVISAKMAR DWNKDQILQA YLNTIYFGRN AYGIGAASKA YFNKDVKDLT
PEEGAILAAS IQAPSRLDPW TNRPEAEARW NYVMDGMVTI GAMNQGQRAA AVYPQVQDPA
LTQQTSVAEG TNGLIKQRVI DELAAAGINE DQVNTGGLKI TTTIDPVAQN AAVDQVHQQF
ASLQQDLLGA VVSVDPKTGG VRAYYGGDDP VGWDHANAGI QTGSTFKIFA LAAYLDQGGS
IYDTFDSSPI QTGDATVTNV GGESCGRCSA AEALKRSLNT SYIRVEKALQ GGPQDVADMA
HRLGVATEIP GLGKTLTENG GPPFDGIALG MYPT
//
