ID A0A097IIV4_9CORY Unreviewed; 732 AA.
AC A0A097IIV4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=CDOO_12950 {ECO:0000313|EMBL:AIT62067.1};
OS Corynebacterium doosanense CAU 212 = DSM 45436.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=558173 {ECO:0000313|EMBL:AIT62067.1, ECO:0000313|Proteomes:UP000029914};
RN [1] {ECO:0000313|EMBL:AIT62067.1, ECO:0000313|Proteomes:UP000029914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAU 212 {ECO:0000313|EMBL:AIT62067.1,
RC ECO:0000313|Proteomes:UP000029914};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium doosanense CAU 212(T) (=DSM
RT 45436(T)), isolated from activated sludge.";
RL Submitted (SEP-2013) 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; CP006764; AIT62067.1; -; Genomic_DNA.
DR RefSeq; WP_018022437.1; NZ_CP006764.1.
DR AlphaFoldDB; A0A097IIV4; -.
DR STRING; 558173.CDOO_12950; -.
DR KEGG; cdo:CDOO_12950; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_1_11; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000029914; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029914};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..245
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 338..592
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 663..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 77985 MW; 379008821C1591B5 CRC64;
MVSHSLTTND AQRASSGRRG ILKWFLIALA VIIALPLIGF AVYYSRIHVP EPNEVSTFQV
SNIYASDSST ELARIVPPEG NRSQIPLSEV PVPVQDAVLA AEDREFWTNQ GFSYIGFLRA
VIGQVTGNES AGGGSTITQQ YVKNVLVGDE RSIERKLKEL VYSVKMTNEW DKETILEAYL
NTVYFGRNAY GIQAASNAYF NKPASELTPE EGAVLAATIQ LPSQMDPWVN PEMAEQRWNY
VLDGMVEMGS LDAAQRAATA YPPTRDPAEY SAYTEASGTN GLIRQHVVEE LATLGISEED
ITTRGLQITT TIDMQTQNAT LDSVNENLSY LADDARAAVV SIDPRNGAIR GYYGGEEASG
WDYANAALQT GSIFKVVGLA AALQQGIPLS AQYSSAPVTL PGGITVGNVT GTCGSCSIEN
ALLNSYNTSF IRLQDDLANT TQDTADMGHA LGIARSLPGV PETLTEDGEQ PYEGIILGQY
VSRPLDMAVA MATLANRGVW HQPHFVERVE TYNGEVLFEF DPGEGERRVS AQVADNVLHA
MGPVAAFSRG NTLAGGRPSA SKTGTAQFGD TGLNKDAWML GGTPQLVTAV WMGTAENTSA
IFDAGGGSMY GSGTPATIWK ETLDAALANQ EVMYFADPVP VQYGGFESPY PYSGGGVPNY
TYAPSPGTNS NPAPTYSAPP VEPSEPQRAP EPAPEPSPVP EPAPAPAPEP VPAPAPAPNP
IEDGLEQLLG NL
//
