ID A0A2A9F118_9MICO Unreviewed; 783 AA.
AC A0A2A9F118;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ATJ88_3185 {ECO:0000313|EMBL:PFG44461.1};
OS Isoptericola jiangsuensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Isoptericola.
OX NCBI_TaxID=548579 {ECO:0000313|EMBL:PFG44461.1, ECO:0000313|Proteomes:UP000224130};
RN [1] {ECO:0000313|EMBL:PFG44461.1, ECO:0000313|Proteomes:UP000224130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21863 {ECO:0000313|EMBL:PFG44461.1,
RC ECO:0000313|Proteomes:UP000224130};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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};
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:PFG44461.1}.
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DR EMBL; PDJJ01000001; PFG44461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9F118; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000224130; 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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 ECO:0000313|EMBL:PFG44461.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 81..269
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 373..685
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 719..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 83259 MW; A07579B4DC522584 CRC64;
MASPESRRIT RTIPATQLVA LLLAFVLAAG AGGVLAAGFV IPAVAGANAA ADATIEIYDD
VPAELEPRPL SQQSRIYASN GRLLATFYYQ NRIVVSLDDI SEYMQHAVIA IEDERFYEHN
GIDARGITRA AVNNLSGDAT QGASTITQQY VKNMLIESAL QDDDPFAVID AHEDSLNRKL
REAKMAVALE KQMSKEEILQ GYLNVAQFGS KSIYGVESAS RYYFDKSAAD LTPVEAATIA
GVTKAPGLFD PTRNPEKAEE RRNAVLQNMW KLGYITTDQR DEGQATPIED TLNVTPTSAG
CQSAKQAAFF CDYVIKEVLL DSAFGETRAD RQELLYRGGL EIHTTLDWKK QKTAFKTIND
AVPEDDDSNL EASIVTVEPG SGEILAMAQN VPYSGTKEAD KASRDTTVNY NADYLHGASG
GLQPGSNFKP VVLAEWLRSG HTLNDRVSAN HNSYTVGNFQ TPCVGSLGYD TWDPRNAEGN
AGGTMSVLQA TYQSVNTAYA SMGYQLNLCD LRHTAFEMGF RPTSKSTPTD EAGPLRTTNV
KEKDIDVVAP MIVGTQETSP LGIASMYATI ASGGTYCKPV AILEVTGPQG ESYDVPQADC
DKNALATNIA NTMVYAMEKV FTDGTARRLG GLADGRPVAG KTGTSQVAAQ TWFTGFTPQL
ATSVWVGSIE SQTEDHTNGM WVNGEYFDPL YGSSVAAPAW KVYMDQIIQG MPVKDFGEPD
PALIGAVSTP TPADDGSDDD DSGDGDSGDS GSDGGDSGNQ GGGNGGGPGN GGGRGNGNGG
SDD
//
