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
//