ID E2SNB2_9FIRM Unreviewed; 406 AA.
AC E2SNB2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:EFP60963.1};
GN ORFNames=HMPREF0983_02572 {ECO:0000313|EMBL:EFP60963.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP60963.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP60963.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP60963.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FemABX family.
CC {ECO:0000256|ARBA:ARBA00009943}.
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:EFP60963.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACTJ01000058; EFP60963.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SNB2; -.
DR STRING; 658659.HMPREF0983_02572; -.
DR eggNOG; COG2348; Bacteria.
DR HOGENOM; CLU_048411_2_0_9; -.
DR BioCyc; EBAC658659-HMP:GMFE-2609-MONOMER; -.
DR Proteomes; UP000006223; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT COILED 243..298
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 406 AA; 47127 MW; F782D8622B8C8655 CRC64;
MQYQFIEQLD AKEHDAFVSS HELCNLLQSS KWGLVKENWK RSIVGVKEQG KLVASCMILI
KPLPLGFSMF YIPRGPVLDY TNAELIAYLL KELKRYARRH HCLFITFDPA VHCNDYTIKE
ANENHYEHID AMIQLLQKQG VVFKGFTKQI DDTIQPRYHA NVYACDDFES TLSKSCKKAL
STVQKKMIEV LPYHIDGVED FAKVMHCTEE RKNIHLRDQE YFKRLLEIYG DDAVIYLAKL
PLAKLYEDTR KRYEQTVKEL EACPENAKKK RFTLEELHAS LSRELRELKE NLQRDGEVAV
VSGALCVKFG STAEILYAGM DDRYKRYMAP YASFYKCMTW SFEHGCKWSN MGGIEGSLKG
GLTKFKANYN PTINEFIGEF DLPVYKSLYS LSQWAMKQRK KALQKA
//
