ID F3MIV8_9BACL Unreviewed; 686 AA.
AC F3MIV8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9412_6319 {ECO:0000313|EMBL:EGG31681.1};
OS Paenibacillus sp. HGF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG31681.1, ECO:0000313|Proteomes:UP000004272};
RN [1] {ECO:0000313|EMBL:EGG31681.1, ECO:0000313|Proteomes:UP000004272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF5 {ECO:0000313|EMBL:EGG31681.1,
RC ECO:0000313|Proteomes:UP000004272};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2011) 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 -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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:EGG31681.1}.
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DR EMBL; AEXS01000174; EGG31681.1; -; Genomic_DNA.
DR RefSeq; WP_009595504.1; NZ_AEXS01000174.1.
DR AlphaFoldDB; F3MIV8; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000004272; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 328..595
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 651..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 686 AA; 75728 MW; 9CEA575A20CA5814 CRC64;
MPGQKKSPKR KRRFVRLATF LFVLLGISII AGGILLAYLF ITPLPVAETS RYSRLLDSQG
DLIATFSSTG HTSEQVNLAD ISPLLIQATL AVEDRKFYDH PGFDMKGMAR AVLVNLQHMD
RKQGASTLTQ QLARNLYLSH EKTWTRKLKE AKFTAQLEMK YTKDQILEMY LNEIYYGHGA
YGIESASLLY FGKSAKNLTL AESAMLAGIP KGPTYYSPYN HKDNAVKRQQ IVLNAMAETG
FITEAEADKA ASAKLALLPQ DRQENKVIAS YFRDYVRGLV TKQLNITDQQ LEQGGLNIYT
TLDPRAQKAA EEAVSEGMDS KSELETALVS IDPRNGHIKA MVGGKNYREN QYNHALAKTR
QPGSSFKPIM YLTAIASKEM TSTSVFNSQP TLFHYDNNRK TYQPSNFGDK YLGEIPMREA
IAASDNIYAV NTIMKIGPDK VADMAKKMGI TSPLEPVPSL ALGTSPVSPL EMASAYAVMA
NSGKRVSPVA VLSITDAAGR SLFTAPEEEG EQVVEPSAAY VMTRMMEGVF ETGGTGNRVS
TLMKRPVAGK TGTTDTDAWL VGYTPELSTA VWVGYDKGRE ISKVDGRRAA PIFAQYTEKA
LENVPPKIFP IPDEVVSAYV DPKTGKLAGA GCPDKMLEVF VKGTEPMEYC DEHEGGEPAK
KANPADAAEK QEERSWWKDF KRWWVE
//
