ID A0A0B5HV50_9ACTN Unreviewed; 747 AA.
AC A0A0B5HV50;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SVTN_17395 {ECO:0000313|EMBL:AJF65905.1};
OS Streptomyces vietnamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF65905.1, ECO:0000313|Proteomes:UP000031774};
RN [1] {ECO:0000313|EMBL:AJF65905.1, ECO:0000313|Proteomes:UP000031774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT genetic manipulable producer of the benzoisochromanequinone antibiotic
RT granaticin.";
RL Submitted (DEC-2014) 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; CP010407; AJF65905.1; -; Genomic_DNA.
DR RefSeq; WP_041129925.1; NZ_CP010407.1.
DR AlphaFoldDB; A0A0B5HV50; -.
DR STRING; 362257.SVTN_17395; -.
DR KEGG; svt:SVTN_17395; -.
DR HOGENOM; CLU_006354_2_6_11; -.
DR Proteomes; UP000031774; Chromosome.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000031774}.
FT DOMAIN 77..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 362..634
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 593..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 79609 MW; C51570859817C75C CRC64;
MAKKRSGGGL TGTQQAAKFL GVSVLAGAVL AGIALPAAGA LGLAAKGTVE GFDEIPSNLK
TPPLSQRTTI LDAEGGLIAT VYSRDRKVVP IDKISPYMQK AIVAIEDGRF YEHGAIDLKG
VLRAINKNAQ SGGVSEGAST LTQQYVKNVF VEEAGDDPEK VAQATQQTIG RKVRELKFAI
QVEEELGKKK ILENYLNITF FGQQAYGIEA ASQRYFSKHA ADLDLGEAAM MAGLVQSPSR
YDPINDIQEA TKRRNMVLQR MADVKDISQA EADAAKAKPI KLKVKTPKNG CITAVDGAGF
FCDYVRKTIL NDPTFGKTAE ERTKLWNLGG LTIKTTLDPR AQAAANEAAI AKVNKDDPVA
ASVVQVQPKT GRILSMGQSR PYGLDQKQHQ TTLNLAVGSK MGGTTYGFQV GSTFKPITAA
AALEKGISPA TSFNDPSQIN MNESQYTRCD GKPAGYANWE VNNEMKSEKG VFDMTSALGK
SINTYFAKLE QMAGLCETLT MAKNVGYERE LGKPLKQIPS ATLGSAESTP LDMASVYATF
ANRGIYCTPV AIESIKAANG DKLNVPQTKC TRAMSDRTAD TINQMLKGVV EDGTGTRAGL
SDRDNAGKTG TTNDRKDAWF VGYTPNLSTA VWVGDDVGEK KSMYDITIGG EYYDKVCGGC
LPGPIWKIAM TGALDAGQTP GFVPVSVPRA EKPKDEEKEG DEGPNKPRKP RDAKPGGTTP
TNPIPGVTFP TDLIGGAGGH GNRKPGH
//
