ID C7Q6L7_CATAD Unreviewed; 752 AA.
AC C7Q6L7;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Precursor;
GN OrderedLocusNames=Caci_5193 {ECO:0000313|EMBL:ACU74052.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU74052.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU74052.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU74052.1; -; Genomic_DNA.
DR RefSeq; WP_015793781.1; NC_013131.1.
DR AlphaFoldDB; C7Q6L7; -.
DR STRING; 479433.Caci_5193; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; cai:Caci_5193; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_0_11; -.
DR InParanoid; C7Q6L7; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000000851; 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 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:UP000000851};
KW Transferase {ECO:0000313|EMBL:ACU74052.1}.
FT DOMAIN 77..245
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 352..593
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 648..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 78131 MW; 710D98DEFAB1583E CRC64;
MALRVIDYPR RGKAGLRHWL PSWRLVASTL IAFVLLVTGG AWAVYASISI PPINETVTQQ
HLTVVDDKGV VLGRRGPEIR QDVPLAQVPV PVQNAFLSAE DRNFWSDGAI SLTGTARALL
NDLGGGSTQG GSTITQQYVK NAYLTDERTL SRKVKEAVIA LKISEKQPKS EILQGYLNTV
YFGRGASGVQ MGARAWFSKD INQLSVAEGA VMAALVNAPS YYELAPKDPS IMAKLQARWN
YVLDGLVTMG KLTPADRAAQ QFPALAPWPR PSSETDNQDE YLIEEAIGEA EQKTGLSREQ
LETGGYTIYT TFDAKMQDAA AAAVKAQITS QLNASKRPVD ADVHTAISTV VPGDGAVRVL
YGGDDYSKEA FNASWQGTLS PGSSFKTFAL AAYLQNGGTV SDTFDGTSPF HLPNSNTVIP
NEGGTSYGDV SVQYALNQSI NTVFVEMGQK IGMTKVADAA RAAGIPVTAQ QQSLPALPLG
VVSTNPEQMA AAYGTFAAHG SQVDPYTVAS VQQGGKTIYA HQSLAKQAFT PQVADQVTQA
LQNVVTNGSG GGAQLADGRD VAGKTGTTDL PGDGSKLGSV WFVGYTPTLS TAVAVWGQTD
GGALTPINGM AGKDTVGGGA VAAPLWAAYM DKAVEGTTAQ KFTFTAQNNQ AAPMNPLSPS
GSTTGTTGAT PGKSSTGLPS PPSPTGTYQP PSPTTTTSSS GGKSTTTTSG GGSTSSKSQP
PSSTRSRPTK PKPSSTSSTG QTGGPLPQSS GG
//
