ID F3Y8U6_MELPT Unreviewed; 409 AA.
AC F3Y8U6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:BAK20924.1};
GN OrderedLocusNames=MPTP_0445 {ECO:0000313|EMBL:BAK20924.1};
OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS 702443).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Melissococcus.
OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK20924.1, ECO:0000313|Proteomes:UP000008456};
RN [1] {ECO:0000313|EMBL:BAK20924.1, ECO:0000313|Proteomes:UP000008456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC {ECO:0000313|Proteomes:UP000008456};
RX PubMed=21622755; DOI=10.1128/JB.05151-11;
RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL J. Bacteriol. 193:4029-4030(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 35311;
RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA Akiyama T.;
RT "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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DR EMBL; AP012200; BAK20924.1; -; Genomic_DNA.
DR RefSeq; WP_013773362.1; NC_015516.1.
DR AlphaFoldDB; F3Y8U6; -.
DR STRING; 940190.MPTP_0445; -.
DR KEGG; mps:MPTP_0445; -.
DR HOGENOM; CLU_048411_1_0_9; -.
DR OrthoDB; 2303924at2; -.
DR Proteomes; UP000008456; Chromosome.
DR GO; GO:0016755; F:aminoacyltransferase activity; 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 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 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008456}.
FT COILED 246..300
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 409 AA; 47661 MW; BE4409CAB6667AA4 CRC64;
MKQFIELSEA EFNLFSTHHP KENYLQTVEM AHLLKIRGWK VNYVGLKNDE QIIAAAMLSG
LPIKFGYYYN IAGGPLMDYE NQEEVEFFIN GLKKYTKERK GLYLNFTPNL VYQYRDSDGN
AIGQPDHKIH NTLMACGLQH DGFKTGYANE NPRIVYTKDL TNITTKELTK TYNRSTRTKV
NKTAKSGIKL RELSRDELPF FENVMHHTAD RQDFHDKDLA YYETLYDSFN GKAHFMVTEL
NFFTYAKDIH EKIEKLNKKI EQLKDIPAKE NQRENAKVEL NALEVRLEEI KDIMKEDIEE
EEILAAGLFI ENAREMLFLF GGMYDRYKNF LSPSYYLQHA MMEKTIEKGL SRYNFYGISG
IYDGSDGVLN FKKGFEGIVE EQVGTYTLVV NTQKYQLYRM LKNLVAKTG
//
