ID F3M662_9BACL Unreviewed; 751 AA.
AC F3M662;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE Flags: Fragment;
GN ORFNames=HMPREF9412_5627 {ECO:0000313|EMBL:EGG37139.1};
OS Paenibacillus sp. HGF5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=908341 {ECO:0000313|EMBL:EGG37139.1, ECO:0000313|Proteomes:UP000004272};
RN [1] {ECO:0000313|EMBL:EGG37139.1, ECO:0000313|Proteomes:UP000004272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGF5 {ECO:0000313|EMBL:EGG37139.1,
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:EGG37139.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEXS01000046; EGG37139.1; -; Genomic_DNA.
DR RefSeq; WP_009590858.1; NZ_AEXS01000046.1.
DR AlphaFoldDB; F3M662; -.
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 Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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; SSF49265; Fibronectin type III; 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 38..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 88..263
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 355..633
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 751
FT /evidence="ECO:0000313|EMBL:EGG37139.1"
SQ SEQUENCE 751 AA; 83228 MW; 23C3219BD916A931 CRC64;
MAGKDNQMSR LNKNKDNSKT SKTTKPNAKK KKGKGKRIAW ALFFTAVIAI FCALAGYLFI
LISGEKLLEQ NQDKLTAYGT SKVYDRNGTL MGELSLQKSD PVKYEDIPEK LIQAFIATED
KRFMEHNGVD MWSIGRAAVK DIMARSMVEG GSTITQQLAK NIFLTRDKTF FRKATEMSIA
LALERQHSKQ EIIEMYLNRI NFGGPYYGIK AASERYFGKS DLKELDLWEM ATLAAMPKGP
SRYNPLKNPD LSKERRAVVL TLMEQQGYIT AEEAAEAKKV DYAYTPPERQ QKYTAFIDYV
MEEAEEKWGL TEDDVNIGGY QIYTTMDVNA QKAMEEEFNN PANFEESPDD VQVEGSMVII
NQETGGIVAM VGGREYTRGG FSRATDSRRQ PGSALKPIVS YAPALESGKF TKDSRLSNKK
QCFGSNYCPN NLHGYSETIG MPEAIQRSEN IPAVWLLNEI GVKTGFDFAQ SLGIKMSEGD
ANLSLALGGM DTGTNTFEMA QAFSAFANGG EFKEAFAIKQ IKDNKGKVVH ENKGSKGKRV
MSETTASQMT DMMRRVVEDG TGKNARISRP VAGKTGTTQS GYKGVSSNRD VWFVGYTPEL
TAAVWMGYDN PDRQHLLKRS SSISASLWGK VMEKAVQGYE AKNFPNVEPV QPPVEEPALS
AVSGLTGSYN GETQTVSLSW NPVQGNVQYR IYRKETSESE YSRILDSLGG TSIEDMSAME
GLTYDYYVTA FDPSTGDESE PSNILQIVAV S
//
