GenomeNet

Database: UniProt
Entry: A0A6N0DUI7_9HYPH
LinkDB: A0A6N0DUI7_9HYPH
Original site: A0A6N0DUI7_9HYPH 
ID   A0A6N0DUI7_9HYPH        Unreviewed;       695 AA.
AC   A0A6N0DUI7;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   18-JUN-2025, entry version 21.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE            EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN   Name=pbpC {ECO:0000313|EMBL:QKP78599.1};
GN   ORFNames=HT051_14840 {ECO:0000313|EMBL:QKP78599.1};
OS   Methyloligella sp. GL2.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Hyphomicrobiaceae; Methyloligella.
OX   NCBI_TaxID=2742204 {ECO:0000313|EMBL:QKP78599.1, ECO:0000313|Proteomes:UP000509225};
RN   [1] {ECO:0000313|EMBL:QKP78599.1, ECO:0000313|Proteomes:UP000509225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GL2 {ECO:0000313|EMBL:QKP78599.1,
RC   ECO:0000313|Proteomes:UP000509225};
RA   Grouzdev D.S.;
RL   Submitted (JUN-2020) 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=2.4.99.28;
CC         Evidence={ECO:0000256|ARBA:ARBA00049902};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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; CP054476; QKP78599.1; -; Genomic_DNA.
DR   RefSeq; WP_174542748.1; NZ_CP054476.1.
DR   AlphaFoldDB; A0A6N0DUI7; -.
DR   KEGG; metg:HT051_14840; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000509225; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR050396; Glycosyltr_51/Transpeptidase.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 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   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000509225};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          69..235
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          312..528
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          608..690
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   695 AA;  74074 MW;  BEB90F4707602751 CRC64;
     MTRRLRPSRL RRALLYSGLG VLFAGAIAGG AVSGFVETLG PAPLGDQVEM SPIVVDREGR
     LLRPYTTKAG RWRLPATVAD VDPRFLDVLL AYEDKRFYAH PGVDPLAMLR AAEQLATQGH
     IVSGGSTLTM QVARLLEPRP RSFEAKARQI VRAIQMERKL GKQQVLSRYL TLAPYGGNLE
     GIRAASLAYF GKEPRRLSLG ESALLVALPQ SPEERRPDRS PKAAQAARDR VLDRIAGSGV
     FSNAEIARAR LEPVPHARKP MPILAPHAAD DAVAAAPETR IHRLTIDKRM QARLEQLAKE
     RADRLGPDIS VAMVALDNAT GAVLARVGTP DYFDKRRAGQ VDLTRAVRSP GSALKPFIYG
     LGFEDGAIHP ATLIKDKPVR FGAYAPENFD MSYQGTVSIR RALQLSLNVP AIAVLDAVGP
     ERLVARLGEV GTPLELPPHE KPGLALGLGG VGVTLSALTQ GYSGIARQGS VMASYERQDQ
     PVPAPKRLIS PVAAWYVADI LRGAPPPENG LPGRIAFKTG TSYGYRDAWS IGFDGARTIG
     VWVGRPDGAP VPGLVGRLSA APILFDAFAR TGPVTPLPPA PDGVLTASTA ELPRPLQRFT
     TDPVTAGSTE QALRILFPPN GASLELSGDL NGALDPVPVK ISGGTPPLTV LVNGAPIDLR
     RPSQAVFFAP DGPGFTRVTV TDAAGHADSV LVRLQ
//
DBGET integrated database retrieval system