ID A0A172TPQ6_9BACL Unreviewed; 353 AA.
AC A0A172TPQ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Lipid II:glycine glycyltransferase {ECO:0000256|ARBA:ARBA00040679};
DE EC=2.3.2.16 {ECO:0000256|ARBA:ARBA00039074};
DE AltName: Full=Factor essential for expression of methicillin resistance X {ECO:0000256|ARBA:ARBA00042933};
GN ORFNames=SY83_08240 {ECO:0000313|EMBL:ANE48797.1};
OS Paenibacillus swuensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1178515 {ECO:0000313|EMBL:ANE48797.1, ECO:0000313|Proteomes:UP000076927};
RN [1] {ECO:0000313|EMBL:ANE48797.1, ECO:0000313|Proteomes:UP000076927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6 {ECO:0000313|EMBL:ANE48797.1,
RC ECO:0000313|Proteomes:UP000076927};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Paenibacillus swuensis/DY6/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-D-
CC Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate + glycyl-
CC tRNA(Gly) = beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-
CC Lys-(N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl
CC diphosphate + H(+) + tRNA(Gly); Xref=Rhea:RHEA:30435, Rhea:RHEA-
CC COMP:9664, Rhea:RHEA-COMP:9683, ChEBI:CHEBI:15378, ChEBI:CHEBI:62233,
CC ChEBI:CHEBI:62234, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.16;
CC Evidence={ECO:0000256|ARBA:ARBA00036801};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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DR EMBL; CP011388; ANE48797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A172TPQ6; -.
DR STRING; 1178515.SY83_08240; -.
DR KEGG; pswu:SY83_08240; -.
DR PATRIC; fig|1178515.4.peg.1638; -.
DR Proteomes; UP000076927; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.630.30; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR038740; BioF2-like_GNAT_dom.
DR InterPro; IPR003447; FEMABX.
DR PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR Pfam; PF13480; Acetyltransf_6; 1.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR PROSITE; PS51191; FEMABX; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000076927}.
FT DOMAIN 165..290
FT /note="BioF2-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13480"
SQ SEQUENCE 353 AA; 41214 MW; 2D4E12E4DD130125 CRC64;
MTSQTEEWND ALRSVGGADI YYSPGYCAMA ENNNEGMARL FVYREQQFII CYAFLMRSIN
DLNLPEVKQL QRNMYDIVTP YGYGGPLCNV KDEEERVSLF ERFGEVFSAY CRMVGIVTEF
VRFHPLFHNE KDYSGVQPTP LRNTVCMDLT SSREDVIDSL TSGCRNRVRY AQKNGVRVSR
EDPAQIKDFI ELYYATMDKN HAHPYYYFSE PYFRDLVQLL DQHVSLFVAR YEGRVIASTF
FLHYNDYVTY HLTGSDKDYL KFAPYNLLIC EAASYFKSLG YKYLHLGGGY GGNDELFRFK
STFSKKAPLD FYIGRKVHNP EIYEMLTRQI QVQDNFFPLY RHSSLGVSTY SRV
//