ID C0BQU3_9BIFI Unreviewed; 422 AA.
AC C0BQU3;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=FemAB family protein {ECO:0000313|EMBL:EEG71856.1};
GN ORFNames=BIFPSEUDO_02748 {ECO:0000313|EMBL:EEG71856.1};
OS Bifidobacterium pseudocatenulatum DSM 20438 = JCM 1200 = LMG 10505.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=547043 {ECO:0000313|EMBL:EEG71856.1, ECO:0000313|Proteomes:UP000003875};
RN [1] {ECO:0000313|EMBL:EEG71856.1, ECO:0000313|Proteomes:UP000003875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG71856.1,
RC ECO:0000313|Proteomes:UP000003875};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bifidobacterium pseudocatenulatum (DSM 20438).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG71856.1, ECO:0000313|Proteomes:UP000003875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20438 {ECO:0000313|EMBL:EEG71856.1,
RC ECO:0000313|Proteomes:UP000003875};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2009) 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:EEG71856.1}.
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DR EMBL; ABXX02000001; EEG71856.1; -; Genomic_DNA.
DR RefSeq; WP_004220142.1; NZ_JGZF01000002.1.
DR AlphaFoldDB; C0BQU3; -.
DR KEGG; bpsc:BBPC_0240; -.
DR PATRIC; fig|547043.19.peg.253; -.
DR eggNOG; COG2348; Bacteria.
DR Proteomes; UP000003875; 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: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 Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
SQ SEQUENCE 422 AA; 47573 MW; C2BB27CF19F0A7D2 CRC64;
MRAFSLVTLS PEAFDDFSAH HADGNFQQTS AAGRLRAGQG IEVEYLGVQE NGTIVAGALF
ETHRSRLSTF SVVHDGPLCD YRDRELTEYF MTQLKQHAKA KGSAQMEIVP EMPYCLHDSR
GGELPADQGG APADDAVETL KNLGFMHDGF TIGYTAVPRW RYLKDLTGIT DEKSLLKSYD
KRTQWSVKRA ASMGVHVREL GEDELQVFAD IEQATAERRN FEYRGEAYFR KFKQAYGSKA
HFMVAQIHIG EYIADMESKC DALRKKVDVL QAKYDEHPTT KTERQLGEES RNLAAAEKRL
TEAAEYAKDG DVLPAAASLF VEHARETVYL FSGSVEKYKP FYASALIQHD AMLHLCVERG
VTRYNFYGIN GVFDDPEDEG RGVLEFKQGF NGYVEELMGS FVLPVRPLTF KLKTALRELL
RH
//
