ID A0A0F7N769_9ACTN Unreviewed; 755 AA.
AC A0A0F7N769;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=AA958_14505 {ECO:0000313|EMBL:AKH83243.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH83243.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH83243.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH83243.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-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};
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DR EMBL; CP011492; AKH83243.1; -; Genomic_DNA.
DR RefSeq; WP_047016558.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7N769; -.
DR STRING; 444103.AA958_14505; -.
DR KEGG; strc:AA958_14505; -.
DR PATRIC; fig|444103.5.peg.3054; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000034283; 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: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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 362..632
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 675..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 755 AA; 80063 MW; 4AD11D016072830F CRC64;
MAYKRPGGGL TATQQAAKFL GVSVLAGSVL AGLALPAAGL LGLTAKGTVA EFDDIPADLK
RPPLSQKTTI LDREGGHLAD VYSRNRTVVE FDDIAPVMRQ AIVAIEDERF YEHGAVDLQG
ILRALNSNAQ SGTVSEGAST LTQQYVKNLF VEEAGNDAQK VAEATRQTLG RKIQELKYAI
QVEKELTKDE ILENYLNIAF FGQQAYGIEA AAERYFSKSA DKLTLAESAM LAGIVQSPSR
YDPINNPEAA EKRRNTVLRR MAGNDNVTRA EADKAMKEPL GLKISEPRNG CITAVSGAAF
FCDYVREVLL DDKGFGKTPE QRVKRWNRGG LTIRTTLDPV AQKSASESIK SHVYQDDAVA
TAVTMVEPGT GKIRAMGQSR PYGSGKNELM INLSVEKSMN GSNYGFQVGS TFKPLTAAAA
LEKGVPNTKV YPSPNEMPYP SPVETCEDGK DWVNTEGSEV ANETEEEVGP YSMREATAKS
INTYFVDLIS EIGICPVKEL AQSMGVHRGD GKDLEESPSL TLGGQTIAPL AMANAYATFA
NRGEYCSPVA IESIKDAKGK KVPVPKTQCK RVMSEKTAGT INTLLSGVVE DGTGKEAGLT
GRDNAGKTGT TDERKAAWFV GYTADLAGAV WVGGPLDDVS MENIQIGPTY HDRVFGGAVP
GPIWRDAMDG ALAGKTSPEL YKVPVPVDRP DKGKGDDDDE DDEDKPENPL GGLLGGSNGN
GGGNGGGGPG GGTLDGGSLD GGWSDGGNGG WPDGR
//
