ID A0A1I3UI29_9RHOB Unreviewed; 677 AA.
AC A0A1I3UI29;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN04488095_3762 {ECO:0000313|EMBL:SFJ82710.1};
OS Jannaschia pohangensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=390807 {ECO:0000313|EMBL:SFJ82710.1, ECO:0000313|Proteomes:UP000199110};
RN [1] {ECO:0000313|EMBL:SFJ82710.1, ECO:0000313|Proteomes:UP000199110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19073 {ECO:0000313|EMBL:SFJ82710.1,
RC ECO:0000313|Proteomes:UP000199110};
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=2.4.1.129;
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; FORA01000008; SFJ82710.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3UI29; -.
DR STRING; 390807.SAMN04488095_3762; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199110; 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:UP000199110}.
FT DOMAIN 58..225
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 298..519
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 594..672
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 677 AA; 71007 MW; 5C2C26158164A584 CRC64;
MRRRGPLLAL ALMVAIGAGW RAFDDWVDRT AVPPLTVATS AEVLDREGAL LRAYTVADGR
WRMAVGAGEV DLLYVAMLIA WEDRRFRDHA GVDPRAVVRA AVQGVRHGTV VSGASTLTMQ
VARLIEDGPT GSWYGKLRQA RLALALERLL TKDEVLAMYL ARAPFGGNLE GVRAASLAYF
GKEPARLTPA QAALLVALPQ SPETRRPDRA PDVARAARDR VLWRMADLGL IDGEARDAAL
AEAVPARRRD FPARAPHLAD RLSAGGRVAT TLDGALQARL ERLATEAVAG QGRRLGIAIL
VADHHSGEIL ASVGSADYDN DARAGFVDMT QALRSPGSTL KPLVYALAFD LGMAHPETLI
DDVPTTFGTW VPQNFDGTFQ GTMRARAALQ LSRNIPAVKL AEGVGPARVM SAIRRSGARA
ELPGGPPGLA VTLGGVGMNL EGLVQLYATL ARGGGRVTLS ALPGQGGPEA GRITGAAAAW
QVGDVLADLV PPSGAEPGDV AWKTGTSYGH RDAWAIGWDG AHVVGVWMGR PDGTPVPGAF
GGDLAAPVMF RAFARIARDR VPLPPAPPET LTVTNAELPA PLQRFSVRGA GLLADADAPA
IAFPPDGAVV VTGGQPLAAQ VRDGRPPFTW LADGRPVAVN ESGRATLVDV ARNGFVTLTV
IDAAGRSART QVRVDGG
//
