ID A0A2Z4FM61_9DELT Unreviewed; 793 AA.
AC A0A2Z4FM61;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 18-JUN-2025, entry version 30.
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:AWV90051.1};
GN ORFNames=DN745_12160 {ECO:0000313|EMBL:AWV90051.1};
OS Bradymonas sediminis.
OC Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae; Bradymonas.
OX NCBI_TaxID=1548548 {ECO:0000313|EMBL:AWV90051.1, ECO:0000313|Proteomes:UP000249799};
RN [1] {ECO:0000313|EMBL:AWV90051.1, ECO:0000313|Proteomes:UP000249799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FA350 {ECO:0000313|EMBL:AWV90051.1,
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.
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 ---------------------------------------------------------------------------
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; AWV90051.1; -; Genomic_DNA.
DR RefSeq; WP_111335206.1; NZ_CP030032.1.
DR AlphaFoldDB; A0A2Z4FM61; -.
DR KEGG; bsed:DN745_12160; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000249799; 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 4: Predicted;
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:UP000249799};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 55..217
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 311..582
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 708..790
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 793 AA; 86558 MW; BEF338A1FC623B5F CRC64;
MKRAMISLAL GAVVAGFSLW SAMWVLPLPQ RLAEADSTVV EWRNGEPAHV FLAPDGRWRL
QTQLKKVDPH YIEALIGYED KRFYTHGGID LRAIVRATTS NIRHGRVVSG ASTLTMQLVR
MVEPRPRTLR SKIIEAFRAA QLEQHLSKDE ILAAYLKFLP FGRNVEGLET AAWMYFGHDA
TALSPAEIAT LLAVPQSPNQ RYPTPKNAAR LRSARADIAA ELLEAARLLR GAAPENLSDA
QALAQIEAQP LPTRLRSMPR EMPHFAIWLR QQYPGVPRLR STIDASTQRT VEKFATSHRG
RIMRLGANNA AVVVIDHESG ALRAALGNFD FDDLINQGQI PGFAVRRSSG SLLKPIILAQ
AIDAGIALPS HLVADVPVDY SGYQPQNYSE EFNGLVRLDD ALSRSLNIPF VRLVERLGVA
PFLEMLRRLG AEGIDPRPGY YGLSVAIGGI SATPLEIAGM YTALARRGER APLYFLKADE
DADYGNAFAY RRGSFSPGAA RLVAEVMSQR GRPDSLALRR IRATPNRYAW KTGTSMGLRD
AWTAGFGAQH TAAIWTGNFD NRGQTGVVGS QAAAPLFFDI MEAVDSGLNF AAMTPESAST
TAIDELSEVE VCAYSGHLPT SACTHKKTVQ IPTDSTPTAP CPFHTLRDID EATGLALNLE
CRQSRPHQTR SYVVWPTSVR RTMKDAGYKL PAKPPGFAPG CGPSGYDTRP SIVSPAPDTV
FALLSDISPA EQMLPLIAET HEAGARFSWF VNGEYLGSAP SGEALWWEPK RGAHEIVVSD
ARGGSARVRV LIE
//
