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Database: UniProt
Entry: A0A8J7LXP2_9BACT
LinkDB: A0A8J7LXP2_9BACT
Original site: A0A8J7LXP2_9BACT 
ID   A0A8J7LXP2_9BACT        Unreviewed;       694 AA.
AC   A0A8J7LXP2;
DT   25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 1.
DT   18-JUN-2025, entry version 16.
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:MBJ6723451.1};
GN   ORFNames=JFN93_01905 {ECO:0000313|EMBL:MBJ6723451.1};
OS   Geomesophilobacter sediminis.
OC   Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia;
OC   Geobacterales; Geobacteraceae; Geomesophilobacter.
OX   NCBI_TaxID=2798584 {ECO:0000313|EMBL:MBJ6723451.1, ECO:0000313|Proteomes:UP000636888};
RN   [1] {ECO:0000313|EMBL:MBJ6723451.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Red875 {ECO:0000313|EMBL:MBJ6723451.1};
RA   Xu Z., Zhang Z., Masuda Y., Itoh H., Senoo K.;
RT   "Geomonas sp. Red875, isolated from river sediment.";
RL   Submitted (DEC-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   -!- 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:MBJ6723451.1}.
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DR   EMBL; JAEMHM010000002; MBJ6723451.1; -; Genomic_DNA.
DR   RefSeq; WP_199382301.1; NZ_JAEMHM010000002.1.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000636888; Unassembled WGS sequence.
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:UP000636888};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          34..197
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          291..510
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          611..687
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   694 AA;  75765 MW;  1559BCEE8CBD3E8D CRC64;
     MSTISAQAAL LPTFSEVQKA HRRSDVLILD RHGELIHELR VDKTGRRLEW TKLKDVSPAL
     VKAVLQSEDR RFYEHGGVDW KAVGAALIDR FFGSKTRGAS TISMQVAVMV QRGGRPLGHK
     TFRQKWDQMA AARELEKSWK KDEILEAYLN LVSFRSELQG IAAASRGLFG KEPSGLDLKE
     SCTLAALIRS PNALPAVVGQ RAALLAQSLS PGEPGEAYRR TAIDALSRPY RLRPYLALAP
     QVAKILTAGA GQGELSAQTI NSTLDLRLQR FALQSLRQQL DLLQGRHVGN GAVLVVDNAT
     GNILAYVGNS GDSQVDGIVA KRQAGSTLKP FLYGLALEKR LLTTASVLDD TPLHISTERG
     IYMPHDYDHR PRGPVTVRTA LSASLNIPAV RTQLLVGTEP FADRLRRVGF DLRRSAEFYG
     FSLALGTADV SLKELVNAYR CIARGGIVSP LHLTPGHSGR TLRAMDPKVA YLVSDILSDP
     GSRSVTFGLD NPLTTRYWTA VKTGTSKDMR DNWCIGFSRR YTVGVWVGNL SGDPMWNVSG
     VSGAAPVWLE VMNYLHGNVR SAPPPRPRGV VAARVPAGHG EAERGELFLA GTEPPSVPAA
     RPAGEAWHIA RIAYPPDGTI IVIDPDIPEP NQRVFFETEN EAPGLKWRLN GELLPPGEEG
     RRWAPRVGRY ELALVDNGGK VQDAVSFEVR GQNQ
//
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