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Database: UniProt
Entry: A0A498DNE0_9ACTN
LinkDB: A0A498DNE0_9ACTN
Original site: A0A498DNE0_9ACTN 
ID   A0A498DNE0_9ACTN        Unreviewed;       780 AA.
AC   A0A498DNE0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=D7M15_09555 {ECO:0000313|EMBL:RLL67068.1};
OS   Streptomyces sp. Z26.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2500177 {ECO:0000313|EMBL:RLL67068.1, ECO:0000313|Proteomes:UP000288048};
RN   [1] {ECO:0000313|EMBL:RLL67068.1, ECO:0000313|Proteomes:UP000288048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z26 {ECO:0000313|EMBL:RLL67068.1,
RC   ECO:0000313|Proteomes:UP000288048};
RA   Buchmann A., Cano-Prieto C., Baz M., Hassani L., Barakate M., Nafis A.,
RA   Niedermeyer T.H.J., Gross H.;
RT   "Draft Genome Sequence of the Novonestmycin-Producing Strain Streptomyces
RT   sp. Z26, isolated from potato rhizosphere in Morocco.";
RL   Submitted (OCT-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:RLL67068.1}.
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DR   EMBL; RCHV01000002; RLL67068.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498DNE0; -.
DR   OrthoDB; 8865355at2; -.
DR   Proteomes; UP000288048; 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: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:UP000288048};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        42..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          92..265
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          367..624
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..725
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   780 AA;  82445 MW;  52B6DF82C5DEDC2E CRC64;
     MSDVPNDMAE GRAESHGPGP DTPGPAAPGA PRRTGWRRLV PTWRIVVGSG LMIVLLLSGG
     LVAGYLLVDI PAPNQSAAAQ NNVYLYSDGT QIARDGEINR ENVTLSQIPK RTQRAVLAAE
     DRNFYNESAV NLKAMTRAGW KMVTGGGKQS GSTITQQYVK NYYLTQEQTV TRKAKEFFIA
     LKLDNEVSKD EILLGYLNSS YFGRNAYGIQ AAAHAYYGKS ATELTVPESA YLAALVNAPG
     AYDTRAHPEN KDRALARWNY VLDGMVEQGW LDEGRRDAMK FPEPGPIKPP NALSGQRGYL
     VEAVKNYIVD NGIVDERRLA SGGFRITTTL DRKKQDALVE AVDKRLMKQL SDDRKVDKFV
     RAGGTSIDPE TGEVVAMYGG KDFVQQYVNN ATRRDYQVGS TFKPFIFTSA VQNDSTTQSG
     QAIRSRTIYD GTNKRQVMSD GQPTDYAPAN EDDRSYGQIP VTTAMDKSVN SVFAQMGVDV
     GPQKVKDTAI DLGVPKDTPN MPADGSIALG VATASTLDMA EAYATYARHG MHRDSSLVKK
     ATRGGEVIKL PGREEKRTVP REAADSTTAM LESVVKGGTA VAAQSAGRPA AGKTGTAEED
     RAAWFAGYTP ELATVISVMG QNPEGGHEPL YGAAGLPRIN GGGFPAEIWG AYTADALKGE
     PVEEFDLETG SDDPGPPTVP PDSGGQTGDT PPGDPTTEPP NTPSDTPEEP SPPEETPPTE
     EPSGPGIPPT GGLEGGATDG STGGDPGGAN GADGGANGDP GGGAVNGDPG GGTIPMGRRD
//
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