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Database: UniProt
Entry: A0A0N0SX13_9ACTN
LinkDB: A0A0N0SX13_9ACTN
Original site: A0A0N0SX13_9ACTN 
ID   A0A0N0SX13_9ACTN        Unreviewed;       650 AA.
AC   A0A0N0SX13;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=ADL01_37800 {ECO:0000313|EMBL:KOV58548.1};
OS   Streptomyces sp. NRRL WC-3618.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV58548.1, ECO:0000313|Proteomes:UP000037738};
RN   [1] {ECO:0000313|EMBL:KOV58548.1, ECO:0000313|Proteomes:UP000037738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV58548.1,
RC   ECO:0000313|Proteomes:UP000037738};
RA   Noorani M.;
RL   Submitted (JUL-2015) 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:KOV58548.1}.
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DR   EMBL; LGDW01000480; KOV58548.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0SX13; -.
DR   PATRIC; fig|1519490.3.peg.8237; -.
DR   Proteomes; UP000037738; 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: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:UP000037738}.
FT   DOMAIN          75..251
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          356..591
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          402..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   650 AA;  70074 MW;  E55BA7C7A5E6AEB0 CRC64;
     MLLARAAALA PKYPRPGRTG WRRWMPSWRQ WLGGALTSIG VSALLLGIAY AATDIPSDLN
     TYATQQDNVY FWADGTPMAR TGWVQRQAMP LNEIPEDVRW SVLAAENASF YSDSGISLKG
     LSRALFRTIG QGDTQGGSTI TQQYVKNVYL NQNQTIGRKF TEAMISLKLD NRMSKDDILE
     GYLNTSWFGR GCYGIQRAAQ AYYGKDVSRL DAGEGAFLAS LLKGAGLYDP TLSSANHARA
     VARWSWTLDR MVKIGKLTKA ERAKFTKFPE PLKRNPLYDT GEQTDYLLEV ASQYAKKAGG
     ISDKDFDLGG YQVYTTFDRA RERKLADSVA KARKKALKGD RNAAKTAHYG AASVTADGRI
     LAVYGGPDHR TQGYNESNST TVPAGSAFLP FVYAAGLEHG VQRRRDDERT RVTGQTLYDG
     DDDVPVMTPE GPYWDRSGKK VAASNDGDRS YGRISLRRAL ELSVNTPFMQ LGMDTGLANV
     RATAEAAGLL PGSIGAQVPA LSTGTSTPSA IRMAGGYTTF IAGGKRTEPY SVRKITRNGI
     GIVLHTPAPT RSISAETAEE VTSALADSFR AAHPVAAASA VGKVTGKAGT TPDDTASWYV
     GTHDFVSTAV VVYRIDLTKS LEPLPLKGLA GTADDSVPYG IWSGAMGPLG
//
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