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Database: UniProt
Entry: V8IC98_STRMT
LinkDB: V8IC98_STRMT
Original site: V8IC98_STRMT 
ID   V8IC98_STRMT            Unreviewed;       410 AA.
AC   V8IC98;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Aminoacyltransferase FemA {ECO:0000256|ARBA:ARBA00016236};
DE            EC=2.3.2.17 {ECO:0000256|ARBA:ARBA00012466};
DE   AltName: Full=Factor essential for expression of methicillin resistance A {ECO:0000256|ARBA:ARBA00032233};
DE   AltName: Full=N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase {ECO:0000256|ARBA:ARBA00030706};
GN   ORFNames=U758_07410 {ECO:0000313|EMBL:ETD97793.1};
OS   Streptococcus mitis 27/7.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1415766 {ECO:0000313|EMBL:ETD97793.1, ECO:0000313|Proteomes:UP000018726};
RN   [1] {ECO:0000313|EMBL:ETD97793.1, ECO:0000313|Proteomes:UP000018726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=27/7 {ECO:0000313|EMBL:ETD97793.1,
RC   ECO:0000313|Proteomes:UP000018726};
RA   Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Karpova I.Y.,
RA   Semashko T.A., Larin A.K., Ischenko D.S., Savinova T.A., Dubovickaya V.A.,
RA   Sidorenko S.V., Govorun V.M.;
RT   "Genome sequencing of Streptococcus mitis strains.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-D-isoglutaminyl-L-Lys-
CC         (N(6)-Gly)-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate +
CC         2 glycyl-tRNA(Gly) = 2 H(+) + MurNAc-L-Ala-D-isoglutaminyl-L-Lys-
CC         (N(6)-tri-Gly)-D-Ala-D-Ala-diphospho-di-trans,octa-cis-undecaprenyl-
CC         GlcNAc + 2 tRNA(Gly); Xref=Rhea:RHEA:30439, Rhea:RHEA-COMP:9664,
CC         Rhea:RHEA-COMP:9683, ChEBI:CHEBI:15378, ChEBI:CHEBI:62234,
CC         ChEBI:CHEBI:62235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=2.3.2.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00023962};
CC   -!- SIMILARITY: Belongs to the FemABX family.
CC       {ECO:0000256|ARBA:ARBA00009943}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00008694}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETD97793.1}.
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DR   EMBL; AYRS01000014; ETD97793.1; -; Genomic_DNA.
DR   RefSeq; WP_001174043.1; NZ_AYRS01000014.1.
DR   AlphaFoldDB; V8IC98; -.
DR   PATRIC; fig|1415766.3.peg.1430; -.
DR   Proteomes; UP000018726; Unassembled WGS sequence.
DR   GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.90; -; 1.
DR   Gene3D; 3.40.630.30; -; 2.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR003447; FEMABX.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   PANTHER; PTHR36174:SF2; AMINOACYLTRANSFERASE FEMA; 1.
DR   PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   Pfam; PF02388; FemAB; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 2.
DR   SUPFAM; SSF46589; tRNA-binding arm; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT   COILED          277..304
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   410 AA;  47167 MW;  EE0BC379B56715B5 CRC64;
     MALITLTKEE FQAYSDQVSS RSFMQSVQMG DLLEKRGARI VYLALKQEGE IQVAALVYSL
     PMLGGLHMEI NSGPIYTQQD ALPVFYAELK EYAKQNGVLE LLVKPYETYQ TFDGEGNPID
     AEKKSIIQDL TDLGYQFDGL KTGYPGGEPD WLYCKDLNEL TEKTLLNSFS KKGKALVKKA
     DTFGIQLKKL NREELSIFKD ITKTTSERRE YSDKSLEYYE HFYDSFGEKA EFVIAILNLG
     EYIQNLIHKQ KELSEKIATS LLLLEQYPDS AQKKKEHKEL ARQYESFEVR KAEARELIKK
     YGEKDLVLAG SLFIYMPQET TYLFSGSYTE FNKFYAPALL QKYVMLESIK RGIPKYNFLG
     IQGIFDGSDG VLRFKQNFNG YIVRKAGTFR YYPSPLKYKA IQLLKKILGR
//
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