ID Q9CCY4_MYCLE Unreviewed; 708 AA.
AC Q9CCY4;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=ponA {ECO:0000313|EMBL:CAC32220.1};
GN OrderedLocusNames=ML2688 {ECO:0000313|EMBL:CAC32220.1};
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631 {ECO:0000313|EMBL:CAC32220.1, ECO:0000313|Proteomes:UP000000806};
RN [1] {ECO:0000313|EMBL:CAC32220.1, ECO:0000313|Proteomes:UP000000806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN {ECO:0000313|EMBL:CAC32220.1,
RC ECO:0000313|Proteomes:UP000000806};
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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; AL583926; CAC32220.1; -; Genomic_DNA.
DR PIR; F87245; F87245.
DR RefSeq; NP_302715.1; NC_002677.1.
DR AlphaFoldDB; Q9CCY4; -.
DR STRING; 272631.gene:17576554; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; mle:ML2688; -.
DR PATRIC; fig|272631.5.peg.5181; -.
DR Leproma; ML2688; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_1_11; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000000806; 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 GO; GO:0050896; P:response to stimulus; IEA:UniProt.
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:UP000000806};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..250
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 344..605
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 708 AA; 75662 MW; 46E6CE60B4FB98AC CRC64;
MPGSRLNRTW LLHLNRQVNW RWVRYSLYLA VVVLLLLPIV TFTMTYFMVK VPRPGDIRTN
QVSTILANNG LEIAKIVPPE GNRVDVNLSQ VPVHVRQAVI AAEDRNFYSN PGFDFRASVR
AVQNNLFGSG DLQGGSTITQ QYVKNALVGS AQHGFDGLMR KTKELVIAIK MSDAWSKDDV
LQSYLNIIYF GRGAYGISAA AKAYFDKPVE QLTCSEGALL AALIRRPSVL DPAINLKGVT
ARWNWVLDGM VDINALSPND RSVQLFPATV PPDQARAQNQ TTGPNGLIER QVVKELFELF
NIDRQTLNTQ GLQVITTIDP QAQRIVEKAV SKYLDGQDPD MRAAIVSIDP HNGAIRAYYG
GADANGFDFA QAGLQTGSSF KVFALIAALE QGIGLGYRVD SSPLTVDGIK ITNNGDESCG
NCNIAEALKL SLNTSYYRLM LKLKNGPQAV ADAAHQAGIV SSFPGVAHTL SEDGKGGPPN
NGIVLGQYET RVIDMASAYA TLAASGVYHR PHLVQKVVNA EGRVLFDAST ADNSGDQRIA
KAVADNVTAA MQPIAGYSRG HNLAGGRPSA AKTGTVQLGD TTANKDAWMV GYTPSLSTAV
WVGTVKDNVP LITASGEAIY GSGLPSDIWK STMDGALEGT PNEGFPKPTE VGGYAGVPTL
APPPPLKKVI QPTIEVAPGI IIPVGPPTTV TVPPTQALPD LTTSTTPP
//
