GenomeNet

Database: UniProt
Entry: A0A3E2YLZ3_9ACTN
LinkDB: A0A3E2YLZ3_9ACTN
Original site: A0A3E2YLZ3_9ACTN 
ID   A0A3E2YLZ3_9ACTN        Unreviewed;       755 AA.
AC   A0A3E2YLZ3;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   Name=pbpG1 {ECO:0000313|EMBL:RGC67249.1};
GN   ORFNames=C5N14_19835 {ECO:0000313|EMBL:RGC67249.1};
OS   Micromonospora sp. MW-13.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2094022 {ECO:0000313|EMBL:RGC67249.1, ECO:0000313|Proteomes:UP000258607};
RN   [1] {ECO:0000313|EMBL:RGC67249.1, ECO:0000313|Proteomes:UP000258607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW13 {ECO:0000313|EMBL:RGC67249.1,
RC   ECO:0000313|Proteomes:UP000258607};
RA   Jahanshah G., Miess H., Busche T., Ruckert C., Kalinowski J.,
RA   Rokni-Zadeh H., Gross H.;
RT   "Draft Genome Sequence of Micromonospora sp. MW-13, a Bacterical Strain
RT   Isolated from the Rhizosphere of Wheat in Iran with antibacterial and
RT   possibly plant growth promotion properties.";
RL   Submitted (MAY-2018) 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:RGC67249.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QKKX01000038; RGC67249.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E2YLZ3; -.
DR   Proteomes; UP000258607; Unassembled WGS sequence.
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   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; PENICILLIN-INSENSITIVE TRANSGLYCOSYLASE; 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:UP000258607};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          94..280
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          386..690
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          705..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   755 AA;  79807 MW;  F1E6DDCE445F5757 CRC64;
     MNYLTIGPGA GRIAAFMAIL GFMPPPRSPL SRLFTVLLAG VLAGLVLAVA ALPGNLLLGF
     AAKSAIGSYA ALPEALRTPT TPQRSYLYAN DGETLITTFY DVNRTDVPLA EIAPVMRQAI
     VAAEDRRFYS HGGADLRGLA RALVANVTGG GTEQGGSTLT MQYVRNVLKT DPNRTAEERQ
     AATEQTVGRK LQEIRYATAL EQRLSKDEIL NRYLNIAYFG SGAYGIAAAS QRYFAKSPAE
     LTLPEAALLA GLVQSPDAYS PIDGDADAAL ARRGYVLDAM AGTGAVTAEQ AAAAKAEKLV
     LSPTRQPNGC TAVAQGHDDW GFFCDYLRQW WLTQPAFGDT VPEREQALRR GGYTVVTSLD
     PKLQATAQQQ ATAVYGYDNK RALPIAAVQP GTGRVLAMAV NRHYSLDPNP DGKVNRPNTV
     NPLVSGGGGV DGYQAGSTFK LFTMLAALES GRQLATGFDA PSRLPTRYAA EGEASCGGKW
     CPANANPQWM DGYRTMWDGF GRSVNTYFVW LAEQVGPAKV VEMAQRLGIT FRADADAAFA
     KDNAANWGSF TLGVAATTPL DLANAYATVA AEGTYCAPLP VVSVTTADGD PVPVGEPSCR
     QVLDADVARA ATDAARCPVG QQTTFGQCDG GTATSVDRIV GRPVAGKTGS SEKNATETFV
     GFTPQVAVAG IAANPDDPSD PVGSAVQARV IDAVARTIRT AVAGQPVRDF TPPSRALAGE
     VHRPAPQPSP PQQQRRQQDQ NLPPDVLRWL NRGRG
//
DBGET integrated database retrieval system