ID A0A1Z2KYT5_9ACTN Unreviewed; 675 AA.
AC A0A1Z2KYT5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-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=SMD11_1519 {ECO:0000313|EMBL:ARZ67180.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ67180.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ67180.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ67180.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-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};
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DR EMBL; CP021744; ARZ67180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2KYT5; -.
DR KEGG; salj:SMD11_1519; -.
DR Proteomes; UP000195755; Chromosome.
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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 95..271
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 450..625
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..33
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 72798 MW; 22B1F4EB0CAD841C CRC64;
MFERRKGAHA RNHAAPARRR RAAPRKRRLR PAYPRPGRQG FRRWVPSWRQ TLGSVLTAGG
LLTALVTIMY VRTEIPADLN AFATQQDNVY YWADGTEMAR TGEVNRQDLD LRKVPEKVRW
AALAAENETF YSDSGISVSG MTRAVTRMVT GGSTQGGSTI TQQYVKNAYL NQDQTFSRKF
TEMFIAIKLD NQMSKDDILE GYLNTSWFGR GTYGIQRAAH AYYGKDVSQL NASEGAFLAS
LLKGAGLYDP ALGPKNHERA VERWKWILDR MVTIGKLSKE ERAGYTTFPE PQAPPKPAGL
TGQTGYLVET ARAYVSAHTE VSDHDFDLGG YQIRTTFEKP RMDALTEAVA EASGRLDAEK
RDADKDVRIG AASVATDGRI VALYGGPGYL KQGFNDANSS VVPAGTSFTP FVYAAALREG
VQKERGKPRT PVSPATVYNG DDKISLLTPE GPYWDRSGKI VKALNDGGKS WGKVTLKEAV
AQSVNTPMMQ LGMDAGLDQV GETAVAAGLL KNSLGQKLPG FSLGTATPSA IRMAGAYGTF
AAGGLHSEPY SVDKLSRNGN PVPVEKPEAE RVLPAKVAGA VDDALREAVL RGSATTARAA
GAGAAGKTGT AQDNKSAWFA GYRDKVSTAV SLSRIDPKSQ ELQPLDGLAG AAKGTLGSTI
PIDIWTKYMT AAPKR
//
