ID F1YXN6_9STRE Unreviewed; 406 AA.
AC F1YXN6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:EGE54284.1};
GN ORFNames=SPB_1365 {ECO:0000313|EMBL:EGE54284.1};
OS Streptococcus parauberis NCFD 2020.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=873447 {ECO:0000313|EMBL:EGE54284.1, ECO:0000313|Proteomes:UP000003732};
RN [1] {ECO:0000313|EMBL:EGE54284.1, ECO:0000313|Proteomes:UP000003732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCFD 2020 {ECO:0000313|EMBL:EGE54284.1,
RC ECO:0000313|Proteomes:UP000003732};
RA Stanhope M.J., Durkin A.S., Hostetler J., Kim M., Radune D., Singh I.,
RA Town C.D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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:EGE54284.1}.
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DR EMBL; AEUT02000001; EGE54284.1; -; Genomic_DNA.
DR RefSeq; WP_003104650.1; NZ_AEUT02000001.1.
DR AlphaFoldDB; F1YXN6; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_2_0_9; -.
DR Proteomes; UP000003732; Unassembled WGS sequence.
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; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR PANTHER; PTHR36174:SF1; 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 Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
SQ SEQUENCE 406 AA; 46428 MW; 782AE5A2FC0676DC CRC64;
MGTNFSYKMG ISTEEHDAFV KASSETNLLQ SSAWAQVKSN WASERIGIYK GNEQVASMSI
LIKPLPLKQS IIYIPRGPVL DYSDKELLAY TFGILKKIGK EKKAIFIKFD PAILYKQYSI
NEVGTESEKA KEIIYNIISA GAKWTGLTME IADSIQPRFQ ANRYLHDNLE TSFPKHTKRL
MKDAIRRGVK VKRSDISEID VFANVVALTE ERKKIALRNK AYFKKLMTIY GDDAYLHLAT
VNIAEHLVTF KSELARVEKD LSETLEHQVK RIKKLSDQKE SLKKYISEFE RYSVKYPDEV
VIAGILSIGY GTSMEMLYAG MNEDFKKFYP QYLLYPKVFQ DAFDNGIAWA NMGGVEGSLD
DGLTKFKANF NPTIEEFIGE FNIPVNPLYY PANALYKLRK TLRNKH
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