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Database: UniProt
Entry: A0A172TPQ6_9BACL
LinkDB: A0A172TPQ6_9BACL
Original site: A0A172TPQ6_9BACL 
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
//
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