ID A0A163XZG2_9BRAD Unreviewed; 712 AA.
AC A0A163XZG2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A4A58_13485 {ECO:0000313|EMBL:KZD21599.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD21599.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD21599.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD21599.1,
RC ECO:0000313|Proteomes:UP000076574};
RA Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT Fed.";
RL Submitted (MAR-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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:KZD21599.1}.
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DR EMBL; LVYV01000045; KZD21599.1; -; Genomic_DNA.
DR RefSeq; WP_068736885.1; NZ_LVYV01000045.1.
DR AlphaFoldDB; A0A163XZG2; -.
DR STRING; 943830.A4A58_13485; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000076574; 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; 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 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:UP000076574};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 326..542
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 625..709
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 712 AA; 76223 MW; EAEA28BB45F3D499 CRC64;
MDGRVQPSHD VGRGRSVNGR GWSCLRKVAV TVSAFVVLSG ATIAAWMASL GPLPLEQARK
ISTTVIDRNG KLLRAYAMTD GRWRLPVDAK TSVDSGYLNI LLGYEDKRFY SHHGVDPLAL
ARAALQLVTR GEIVSGGSTI TMQLARLIEP RQQRSISAKI RQAVRALQIE RQMSKDQILD
LYLALAPFGG NLEGLRAASI AYFGKEPKRL SLAESALLVA LPQSPEHRRL DRHPGNARVA
RDRVLERMVG EGRVSAADAM QAKSVSVPKL RKPMPILAPH SADQATSLHK DRSIIRLALD
AGIQRALEGL ARDRAATLGN NISIGLIAVD NESGDVLAHV GSPDYFDDRR AGQVDMTRAV
RSPGSTLKPF IYGLAFEDGF VHPESLIEDR PVRFGSYAPE NFDMSFQGTV PVRKALQLSL
NVPAIALLDR VGASRLSSRL KQAGGNLVLP PGEAPGLAMG LGGVGITLQD LVQLYTGVAR
LGSSKPLREI MQANGGDDRE SLRLMDPVAA WQVGNVLIGT PPPENAAHNR IAFKTGTSYG
YRDAWSVGFD GRMTIGVWVG RPDGAPVPGL VGRTAAAPIL FDAFARTGKL PAPLPKAPKG
VLMASNAKLP LPLRRFRPVG ELIRTGSDQA LHIQFPLNGS RIDASGGEGQ LSAVPVKVAG
GVLPMTVLVN GMAAGELDSR RQRLVDPPGP GFVRLTVMDA MGTADTVVVR IQ
//
