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Database: UniProt
Entry: A0A126YY90_9MICO
LinkDB: A0A126YY90_9MICO
Original site: A0A126YY90_9MICO 
ID   A0A126YY90_9MICO        Unreviewed;       711 AA.
AC   A0A126YY90;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=AX769_02360 {ECO:0000313|EMBL:AMM19184.1};
OS   Frondihabitans sp. PAMC 28766.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM19184.1, ECO:0000313|Proteomes:UP000070552};
RN   [1] {ECO:0000313|EMBL:AMM19184.1, ECO:0000313|Proteomes:UP000070552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA   Park H.;
RT   "Complete genome of Frondihabitans sp.";
RL   Submitted (FEB-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};
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DR   EMBL; CP014513; AMM19184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A126YY90; -.
DR   STRING; 1795630.AX769_02360; -.
DR   KEGG; frp:AX769_02360; -.
DR   Proteomes; UP000070552; Chromosome.
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: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   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   4: Predicted;
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:UP000070552};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..711
FT                   /note="peptidoglycan glycosyltransferase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038704969"
FT   DOMAIN          60..253
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          360..614
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          677..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        690..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  74260 MW;  5F8E6A3A986149E9 CRC64;
     MSVAAGTLVA VGAAPVVAVA GQGAGAAIQA FDDIPEFIEI GKLQQRNVLY ANKGGQQVPF
     ATLYSENRVN AAWGDVAQTL KDAAVAGEDR RFYEHGAVDL NSLARAAVGS IAKSSFGAAG
     GGSTIAMQLV RNVLIAQADS VSDEKKRQAA LAQATEETPR RKVAEMKLAI GLEKKYSKDE
     VLLAYLNIAY FGDHAYGVEA AAQHFYGKGA KALSAAEAAS LLATVQYPET RNMSTPKNYT
     ANTARRDVIL KSMLAEKKID RAAFDAAVAS SVGSYVHLTP ATQGCMAVTE PGAQQWCDLI
     RRQVTSLPSL GATAAERERN WRVGGYQVHT TLDLDQTADA KGQVDTYAPN TETRYDLGGV
     VTSIEAKTGR VLVMAQNKDF NETADGGGST SSAINYAVDH DLGGGNGFQP GSTYKPFTLL
     EWLKQGHRLG ETVNAAPRDF SPNTVCGSRD YTSFRPKNDD GGNPGSVSVR QATARSINTA
     FAAMAQKLDL CDIRETAKSL GVHSADGADL VAYPSATIGS GNTVAPLTMA AAFAGIANGG
     EFCTPVMIDS VTDSEGKKLA GQAQHCEQAI DPTVAAKAAS ALQGPFASGT ATAANPHDGV
     PILGKTGTTD GAEQTWLVGG STNVVTAAWV GNLTGHQNQY RIYGAYGAMN QQRLTIWKHV
     QRSLNAAYGG DAFAAAPQEY TPRAPKITPP TSSPDSDGDG ESSTDTSTPA G
//
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