ID A0A1Q9UR73_9MICO Unreviewed; 746 AA.
AC A0A1Q9UR73;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BJF86_05235 {ECO:0000313|EMBL:OLT40205.1};
OS Serinicoccus sp. CNJ-927.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Serinicoccus.
OX NCBI_TaxID=1904970 {ECO:0000313|EMBL:OLT40205.1, ECO:0000313|Proteomes:UP000186856};
RN [1] {ECO:0000313|EMBL:OLT40205.1, ECO:0000313|Proteomes:UP000186856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-927 {ECO:0000313|EMBL:OLT40205.1,
RC ECO:0000313|Proteomes:UP000186856};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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:OLT40205.1}.
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DR EMBL; MKKF01000044; OLT40205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9UR73; -.
DR Proteomes; UP000186856; 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 PRINTS; PR01217; PRICHEXTENSN.
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 43..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..268
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 366..606
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..700
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..746
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 746 AA; 79486 MW; 697E50A319B0ABB8 CRC64;
MPGRPQAPGH NGGVSSSSTT PRSRRPSGTR KRRGGRRGVI RRVLLWITGL GLLAVLLAVG
VFAWAYARTD VPEPNDFAEA QSSILYYADG ETELARFTGG YDRESVPLSE VPEHVRYAML
SAEDRSFYEN EGVSVTGTAR GAWRTLTGDG LQGGSTITQQ YVKNYYLTAD QTLQRKFTEI
IIAIKIDNEL AKDEVLENYL NTIYFGRGAY GIQTASRAYF DKDVSELDVE EGAFLTGVTN
APSLFDPDYA EGNDERAQER VAYILDGMVE EGWLDASERD GLGLPEIQEP QPSTAAQGVE
GYIAQEARDE LKEVLGVDDA EIDGGGLRVT TTIEQDHQEA AAEAVELYRP TGEGTDDITV
ALTSVRPGDG AVTAMYGGED YQETQLNAAT DAQVQAGSLF KPVTLLAAVQ EGVDTLQTFE
GPTPMSFGDT GDLEVNNFRD LSFGVIDLRI ALAESVNTIY VQLNEQIGPE ATRQAAVDLG
LPEDTPGLDT DLTNVLGTAS PTLLQMTNAY ATIAAEGERA TPYLVTRVET VAGDTTYEAE
PETTQAVDRD AAVDVTDAMT YVVEQGSGMS AGELGRPAAG KSGTSERNVS AWFDGFVPQL
AAGVVMYKGD GTVPMQDVAG IDQITGGTFP AQVWGEFMRQ AMEGEEIQEF SPRVGTSGPT
GTPAPTTQAP APEPTTSEET TEPTETTSEE PTETTSEEPT ETTSEEPTTT EPTESSPAPT
TPAPTSPAPT PTSPDPTEGS SPSPTG
//
