ID A0A239IP73_9RHOB Unreviewed; 747 AA.
AC A0A239IP73;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05421757_104485 {ECO:0000313|EMBL:SNS95359.1};
OS Tropicimonas sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNS95359.1, ECO:0000313|Proteomes:UP000198426};
RN [1] {ECO:0000313|EMBL:SNS95359.1, ECO:0000313|Proteomes:UP000198426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29339 {ECO:0000313|EMBL:SNS95359.1,
RC ECO:0000313|Proteomes:UP000198426};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZOY01000004; SNS95359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239IP73; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000198426; 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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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:UP000198426}.
FT DOMAIN 131..317
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 405..642
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 80398 MW; 83AA9F2258E322FE CRC64;
MSSKGGKRPV LRADKRPTKA TSRGTTAKKP AASASKVSKR KAAPRKSRRV GATARPRGPI
GWLRRLIGFV LGLIWSLTWR SAAVVGLVLG GAVLYFYAQL PPFTDLIDGR TRGSVTLMDR
EGDVFAWRGE QFGSITDINQ VSPNVKNAVV ATEDRRFYWH LGVSPRGVAS AIRINLSEGR
SALSGHGGST LTQQTAKLLC LGVPYDASVW KTEAAYEDDC RRTTIWRKVK EAIYAMAMEA
KYTKDEILVI YLNRAYLGAS ARGFEAAAQR YFGVPASQLD PGQAAMLAGL LKAPTRYAPT
NNLQRAQDRA DTVIKLMYDQ GYITAAERDR AWDRPATLSA AAESNTGGYF ADWVMDTGPN
FLTRDTTEDV LLFTTIDQRI QKAAEGAMRD VFESKLKEGS EAQAAIVVMS ADGAVRAMVG
GRETQVSGAF NRATMAKRQT GSSFKPFVYA AAMDLGYTPL ATVVDEPYCI NVPGSGDYCP
KNYSREFKGR VTLSDALKES LNIPAVKVSE AVGRENVRKI ATEFGIDNAL ANGPALALGV
SESTLVEMTG AYAGILNGGR SVTPYGLNEL RLQGENETLM GQGGGFGERV ISEQAARYLV
YMMSQVIDGG TGQRAKLGDR PAAGKTGTTQ AARDAWFIGF TADYVAGVWM GYDDNTPLSG
VTGGGLPADI WRETMLRVHE GVPISPLPMD VPQAPAGVAA PQYQGNTTTA NSNGAGRQQA
PAQAEQKDNL AERVLQDVLG NLFGRRN
//
