ID A0A1I7N2V8_9HYPH Unreviewed; 709 AA.
AC A0A1I7N2V8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 28.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=SAMN05216456_0640 {ECO:0000313|EMBL:SFV28958.1};
OS Devosia crocina.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Devosiaceae; Devosia.
OX NCBI_TaxID=429728 {ECO:0000313|EMBL:SFV28958.1, ECO:0000313|Proteomes:UP000199074};
RN [1] {ECO:0000313|EMBL:SFV28958.1, ECO:0000313|Proteomes:UP000199074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPL20 {ECO:0000313|EMBL:SFV28958.1,
RC ECO:0000313|Proteomes:UP000199074};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FPCK01000001; SFV28958.1; -; Genomic_DNA.
DR RefSeq; WP_092420816.1; NZ_FPCK01000001.1.
DR AlphaFoldDB; A0A1I7N2V8; -.
DR STRING; 429728.SAMN05216456_0640; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199074; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199074};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..247
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 324..550
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 626..705
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 709 AA; 75328 MW; 7AADF3394149982C CRC64;
MSRIDVPSAP KQPRPWVARL TLLAFSIFVL TLAGVIQLVS WVTTIEAGLP PAPQLQSIPV
SVSVVDRDGL LLRPFTTADG RWRLPAQRTD VDKRFIDMLI AYEDRGFGSH EGIAWSSMVR
AAGQFLGAGG RVVSGGSTLT MQVARLLEGQ STRNAWGKLR QMVHAKRLEA DLSKDEILDL
YLTLAPYGGN IEGIRAASLA YFGKEPARLT TAEAALLVAL PQSPEARRPD RDPEAALASR
NMVLDRLVAT GTIAAEEARA AKLEPIPDAR RQFPMLAAHM ADAAVRSQRG TAEVALTLDK
RLQEALERLA TARSRLIDPR VSVAILAADI ETGEVLASVG SAGLFARESA GFVDMTTAIR
SPGSTLKPLI YGLAFELGLA HPQSLIEDRP TAFGGYVPVN FDGFNRGTVT IHDALTESLN
IPAVVVLDAV GPARLVSRLR RAHANPRLPV DTAPSLAVGL GGVGISLRDL VSLYAAIGNG
GESVRLHDGI APAMETDRTA SVLDPVSAWY VADILADVPP PLNGSPGRVA YKTGTSYGYR
DAWSIGFDGK TVIGVWVGRP DGAPVPGLSG ITAAAPILFE AFDRLGARRS PLPRAPVGVL
HAANPDLPLP LRRFRHPNQD MVARVASPEI AFPADGVDVD LGLVSGAEAS LVVKVRNGVP
PFTFFANGAP FGRSHFARQD AWSPDGPGYV TLSVVDAEGR GDSVTVFLN
//
