ID U2SYQ8_LEIAQ Unreviewed; 762 AA.
AC U2SYQ8;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=N136_03283 {ECO:0000313|EMBL:ERK70378.1};
OS Leifsonia aquatica ATCC 14665.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1358026 {ECO:0000313|EMBL:ERK70378.1, ECO:0000313|Proteomes:UP000016605};
RN [1] {ECO:0000313|EMBL:ERK70378.1, ECO:0000313|Proteomes:UP000016605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14665 {ECO:0000313|EMBL:ERK70378.1,
RC ECO:0000313|Proteomes:UP000016605};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERK70378.1}.
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DR EMBL; AWVQ01000463; ERK70378.1; -; Genomic_DNA.
DR AlphaFoldDB; U2SYQ8; -.
DR PATRIC; fig|1358026.3.peg.2768; -.
DR HOGENOM; CLU_006354_2_6_11; -.
DR Proteomes; UP000016605; Unassembled WGS sequence.
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:UP000016605}.
FT DOMAIN 82..293
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 400..656
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 720..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 762 AA; 80307 MW; 0497FA4A1F9B3849 CRC64;
MTPMASTTRR RWKWAPALVG FVALSGIAGI LAAAAVTPAV ALTGSAADST IDVFDGLPEY
IKVEPLAQAS TMYASSNGQE VPIATFYSQN RVEVGWDAIS QNLKDAAIAT EDPRFYEHGG
IDVTGTLRGA VLTALHKSVQ GGSSITQQYV KNILVQRCEN KQPDLTATAE VQKKQLAAYK
ACYNDATEVD PVRKLKEMRY SIGLEKEYSK NDILQSYLNI ALFGGRVYGV QSAASYYFGV
SAKDVNLQQA ATLIAILNNP DNLRIDQPDS KENGAANGYK ETLDRRNYVL DRMLVNGKIT
KEEHDAARAT PVEPKITPVQ NGCMTAQQYN AAFFCDYVER TIEQNATFGK TDDERSSFLT
RGGLKIYTTL NLDLQNQAQS ALSAYIPPTS PRLDLGAANV AVEVGTGRVI TMVQNRPYDN
TAQPAPGTTA VNYNTDSDMG GSQGFQTGSS YKAFDLLEWL QEGHSLYQTV SGTQHSFPQS
SFHASDPCND IGGAPWNVSN DEGETVGSTT VMNATAQSIN TIFAKMATQL DLCGIKERAQ
DLLVHGADES INPFMSNPSA VLGTNYIAPL TMATAYAGIA NNGVACSPVA IDKIVDADGS
EHAVPKTQCS TTPIDPGVAA AAIYALQGVL RGGGTASSAN PGDGIPIFGK TGTTDNSLEN
WLVTSTTKTA QATWVGNVSG DVALRSQNFN GVGGGNVKFS IVKPIVAALN AAYGGSAFPT
PPSKYVASAP APKPSTPTAP AQPGTGTGPG TGGQGANPPG RG
//
