ID A0A0M8VCX6_9ACTN Unreviewed; 907 AA.
AC A0A0M8VCX6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=ADK64_19945 {ECO:0000313|EMBL:KOV63421.1};
OS Streptomyces sp. MMG1121.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV63421.1, ECO:0000313|Proteomes:UP000037687};
RN [1] {ECO:0000313|Proteomes:UP000037687}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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};
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:KOV63421.1}.
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DR EMBL; LGDV01000190; KOV63421.1; -; Genomic_DNA.
DR RefSeq; WP_053660808.1; NZ_LGDV01000190.1.
DR AlphaFoldDB; A0A0M8VCX6; -.
DR STRING; 1415544.ADK64_19945; -.
DR PATRIC; fig|1415544.3.peg.4297; -.
DR OrthoDB; 8865355at2; -.
DR Proteomes; UP000037687; 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:UP000037687};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 136..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 187..360
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 573..743
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 907 AA; 96046 MW; 21F4CB06659D08FB CRC64;
MSEHRRKPPQ PQGGGRAAAR RGQSGSSSGR RAAPRGATGS PADSYGSSSY GSDNGPGGEE
RPYGSRAEAR RAAQRGNRRR GADNTGPGGR RGGPGGPNGP GRGRGRATSA PGKKRFIDYP
RGEKFGWRRW VPSWKLVTGL FIGFIGSLVA VAGIGYAMVS VPDVAKIAQA QNNVYYWSDK
SVMVATGGEV NRQIINYADI PKEMQYAVIS QENKTFETDS GVDPKGIARA VFNMARGGET
QGGSTITQQY VKNAMLNDQS QTISRKFKEI FVSIKVGAEV PKDQIMAGYL NSAYFGRGAY
GLEAASRAYF NKDAKDLNPG ECAFLAAMLK GATYYDPAGA ISLDAMATPQ ANQKRALAQM
QDTLDKMVQY GHLGAAQRAQ YRTLPKWQNP RSNSRLSGQI GYLVDLAKSY LVNNTAQTGI
TADKLAQGGY RIYTTFDKKK VHELESAVTN VQKANIKPTL RPKTDTHVQF GGASVDPSSG
AIRAIYGGED ATKHFTDNAD STGAQVGSTF KPFVLAAAMK WGVRNPGLGP EQAQDERTQA
SPKSLYSGQN KLKIKTYNGS VWTDKDGKEW LQTNDGNESV GNPPNYKIDL REAMRLSVNS
AYVQLGMDVG LDKVKETALD AGLLKGSLAS SDYPSFSIGT SDPSAIRMAG AYATFAASGK
QNSPYSVDTV EDKDGQVFKH QTQTQEAFTS AVADNVTDVL KTVVDKGTGT NAQLPGREVA
GKTGTTDGNK SAWFVGYTPQ LSTAISMFRL DDNANNKART FLEMYGTGGQ EKIHGASFPA
EIWHDYMAQA LQGAPVMTFP TPPSIGKVIN ADPSPTPTPS VSQSQSQSPS PTPTPSNTAT
SPSPSASDTC QWSWGNPCNG ASNGGTDTGG TTGGTSPSPT ATETTGNGGN TRGNGNGNGG
IFAGQNG
//
