GenomeNet

Database: UniProt
Entry: A0A2Z4FLY7_9DELT
LinkDB: A0A2Z4FLY7_9DELT
Original site: A0A2Z4FLY7_9DELT 
ID   A0A2Z4FLY7_9DELT        Unreviewed;       711 AA.
AC   A0A2Z4FLY7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   Name=pbpC {ECO:0000313|EMBL:AWV89688.1};
GN   ORFNames=DFR33_102203 {ECO:0000313|EMBL:TDP76571.1}, DN745_10185
GN   {ECO:0000313|EMBL:AWV89688.1};
OS   Bradymonas sediminis.
OC   Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae; Bradymonas.
OX   NCBI_TaxID=1548548 {ECO:0000313|EMBL:AWV89688.1, ECO:0000313|Proteomes:UP000249799};
RN   [1] {ECO:0000313|EMBL:AWV89688.1, ECO:0000313|Proteomes:UP000249799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FA350 {ECO:0000313|EMBL:AWV89688.1,
RC   ECO:0000313|Proteomes:UP000249799};
RA   Guo L.-Y., Li C.-M., Wang S., Du Z.-J.;
RT   "Lujinxingia sediminis gen. nov. sp. nov., a new facultative anaerobic
RT   member of the class Deltaproteobacteria, and proposal of Lujinxingaceae
RT   fam. nov.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TDP76571.1, ECO:0000313|Proteomes:UP000294609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28820 {ECO:0000313|EMBL:TDP76571.1,
RC   ECO:0000313|Proteomes:UP000294609};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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   ---------------------------------------------------------------------------
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; CP030032; AWV89688.1; -; Genomic_DNA.
DR   EMBL; SNXT01000002; TDP76571.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2Z4FLY7; -.
DR   KEGG; bsed:DN745_10185; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000249799; Chromosome.
DR   Proteomes; UP000294609; 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: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; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR011815; PBP_1c.
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; 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   Reference proteome {ECO:0000313|Proteomes:UP000249799};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          61..229
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          318..594
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   711 AA;  78479 MW;  ABA96147A4284FB2 CRC64;
     MKRRAKIPLI LAVVCGVCAL FFGAWVWFTP FDDRLLSAQN ITSTRIVDRY GRGLREVLGS
     SQGRARQVEL EQISDHLINA TVHAEDRRFW AHSGVDPLAI GRASWQNMRN LEVISGASTL
     TQQVVKLLRS GNASRNLLNK FSEAVLAIRL EKSASKQEIL AQYLNRAPYG NQLFGVSAAS
     WMYFDKPPAQ LSLAEAALLA GIPRAPSLYN PYEDLAGAKK VQERILNLMR ERGVISAIQY
     ETAVAEKLVI LRPDRRVLAP HFSEYVLTEL RNRGAEDDLN AHPKLIRTTL DLDLQKTVQD
     IVRAELSLLE KKNVHQAAVV ILDTQTSEVL AWVGSQDYWA EEHGGANDGV LALRQPGSAL
     KPFVFGAFFE QGYRAAETLA DFPTEFPTEK GVYIPKNYDR AYHGPVSARA ALASSLNIPA
     VMVAQTVGVK KVLDTLRDFG MDTFDQDDAH YGLGVALGNG EVRLRDLTAA YATLGRLGTR
     KELRIFLDDA LPAPTKPTFR TSVKDAQIFS PETAYILMDI LSDDAARAQG FGRYSALYFP
     YRVAAKTGTS DGFRDNWTFA VTPEYTIGVW AGNFDASPMQ RSSGITGAAP IMRQVTQALY
     PDAANAGDVP WFPRPDAVET HRVCTLSGHK PGPHCPTTRL ELFSAEAAPE EACAIHKSLA
     IDTRNGLLAS PECPAEFVRD EVFTSIPPDW VDWARRRGER LPPTRTSGLC H
//
DBGET integrated database retrieval system