ID Q8NTM8_CORGL Unreviewed; 795 AA.
AC Q8NTM8; Q6M883;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Membrane carboxypeptidase (Penicillin-binding protein) {ECO:0000313|EMBL:BAB97671.1};
GN OrderedLocusNames=Cgl0278 {ECO:0000313|EMBL:BAB97671.1};
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627 {ECO:0000313|EMBL:BAB97671.1, ECO:0000313|Proteomes:UP000000582};
RN [1] {ECO:0000313|Proteomes:UP000000582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC NCIMB 10025 {ECO:0000313|Proteomes:UP000000582};
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
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; BA000036; BAB97671.1; -; Genomic_DNA.
DR RefSeq; NP_599531.1; NC_003450.3.
DR RefSeq; WP_011013529.1; NC_006958.1.
DR AlphaFoldDB; Q8NTM8; -.
DR STRING; 196627.cg0336; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; cgl:Cgl0278; -.
DR PATRIC; fig|196627.13.peg.282; -.
DR eggNOG; COG0744; Bacteria.
DR eggNOG; COG2815; Bacteria.
DR HOGENOM; CLU_006354_2_6_11; -.
DR OrthoDB; 9766909at2; -.
DR BioCyc; CORYNE:G18NG-9834-MONOMER; -.
DR Proteomes; UP000000582; Chromosome.
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 CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03793; PASTA; 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.
DR PROSITE; PS51178; PASTA; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:BAB97671.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000582}.
FT DOMAIN 686..751
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 750..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 82954 MW; 52DAFBF4BE3C7AB4 CRC64;
MSTTNSLTKL VASTVAAGVL GALALVPFAS LSGVAVARTN DTMQTNLSDL TDGRGPGVTT
ITDSTDQPIA YIYAQRRFEV GGDQISTSMK DAIVSIEDRR FYEHDGVDLQ GFGRAILTNL
AAGGVEQGAS TINQQYVKNF LLLVEADDEA EQAAAVETSI PRKLREMKMA SDLEKTLSKD
EILTRYLNIV PFGNGAYGVE AAARTYFGTS AAELTIPQSA MLAGIVQSSS YLNPYTNHDA
VFERRNTVLG AMADAGAISP DEASAFQQEP LGVLETPQGL SNGCIGAGDR GFFCDYALQY
LSEQGITQDM LAKDSYTIKL TLDPDVQDAA HNAVSSHVDP TTPGVAEVVN VIEPGENSRD
ILAITSSRNY GLDLDAGETM LPQATSRVGN GAGSIFKIFT AAAAIQQGAG LDTMLDVPSR
YEVKGMGSGG AANCPANTYC VENAGSYAPR MTLQDALAQS PNTAFVEMIE QVGVDTVVDL
SVKLGLRSYT DEGSFDGESS IADYMKDNNL GSYTLGPTAV NPLELSNVAA TIASGGMWCE
PNPIASVHDR EGNEVYIDRP ACERAIDAET ASALAVGMSK DTVSGTAASA ASMYGWSLPT
AAKTGTTESN QSSAFMGFNS NFAAAPYIYN DGTSTTPLCS GPVRQCSSGN LFGGNEPAQT
WFNMASNVPA ASQGTLPSSS DSFRLGTSGE LLNQVVGQSE ASARRTLEAK GYKVTTRSVS
GAGSARGTVV SATPQGAVLI DGGTVILDIS DGTSPAPAAT NNDDSDDGDT PAPSTNNRGT
TIEDAINDAI NQFFR
//
