ID A0A1N7KYW8_9RHOB Unreviewed; 678 AA.
AC A0A1N7KYW8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05421795_102328 {ECO:0000313|EMBL:SIS66785.1};
OS Phaeovulum vinaykumarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Phaeovulum.
OX NCBI_TaxID=407234 {ECO:0000313|EMBL:SIS66785.1, ECO:0000313|Proteomes:UP000186098};
RN [1] {ECO:0000313|Proteomes:UP000186098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18714 {ECO:0000313|Proteomes:UP000186098};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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}.
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DR EMBL; FTOM01000002; SIS66785.1; -; Genomic_DNA.
DR RefSeq; WP_076364039.1; NZ_OBMN01000002.1.
DR AlphaFoldDB; A0A1N7KYW8; -.
DR STRING; 407234.SAMN05421795_102328; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186098; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000186098}.
FT DOMAIN 70..225
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 301..510
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 595..672
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 678 AA; 70175 MW; ABEB08BEFF480AA1 CRC64;
MGARGLGRAL GALALVLGLA AGARDGLDGW IAATEIPVAA PVGTEIVDRD GRLLRAFAVE
DGRWRLAPGP VDPDFLRLLI AIEDRRFASH AGIDPLALAR AAGQAVLAGR IVSGGSTLTM
QVARLLENGP TGSWAGKARQ MRVALALERR LGKDEILDLY LRLAPYGGNL EGVRAASLAY
FGHEPAHLTP AEAALLVALP QAPEARRPDR APAAARAARD RILARAAALG VIAPAYAEHP
EPLPRARAEF PALAPQLAAR LAAGAAPGAR IETTLDADLQ AALERLAARA VAGLAGRVSA
AIVVADHRSG EILAQVGGAD WGDSGRAGYL DLSTAERSPG STLKPFVYAL AFDDGLAHPE
TLIDDRPTAF GGWRPQNFDH IFRGRVSLRA ALQASLNIPA VALTEAVGPA RLMATLNRAE
AGLRVPQGAP GLAIVLGGAG ISLRGLTQAY AGLARLGRPI RLSVHPGQAQ PLPGRMFGAV
AAWQVGHVLA EAVPPGGGPR GQIAWKTGTS YGHRDALALG YDGAHVAGVW LGRPDGTPVP
GAFGAGLAAP ILFEVFGRLG ARVALPPPPP ATLMLDNAHL PQPLRQFRGR EAAFARTDPA
GPQMAFPPPG ARIAARGGLG VRITGGTAPF TWLANGAPVA VAERRREVIL PLAGPGFVQL
SVIDAEGRST RTEVELLP
//
