ID D5Q9H8_CLODI Unreviewed; 331 AA.
AC D5Q9H8;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=BioF2-like acetyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF0220_3562 {ECO:0000313|EMBL:EFH05483.1};
OS Clostridioides difficile NAP08.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=525259 {ECO:0000313|EMBL:EFH05483.1, ECO:0000313|Proteomes:UP000003227};
RN [1] {ECO:0000313|EMBL:EFH05483.1, ECO:0000313|Proteomes:UP000003227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP08 {ECO:0000313|EMBL:EFH05483.1,
RC ECO:0000313|Proteomes:UP000003227};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (MAY-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:EFH05483.1}.
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DR EMBL; ADNX01000098; EFH05483.1; -; Genomic_DNA.
DR RefSeq; WP_003421004.1; NZ_GG770715.1.
DR AlphaFoldDB; D5Q9H8; -.
DR HOGENOM; CLU_073603_0_0_9; -.
DR Proteomes; UP000003227; 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; 3.40.630.30; -; 1.
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); 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 331 AA; 39335 MW; 275346F977535578 CRC64;
MNNIRINKFE KSCEKHWDYF VENKSINGTF LQTRNFLNYH EEGKFTDHSL IIYKGEEILA
VVPACEIYEN GERIFFSHLG STFGGIIIRS GFNDIRHVNA ITNKLEIYLQ EQSFNKVYLK
NTSRIFCKED TSLLEYFLFK NNYMFYDELS MFLELSKYKE DIVANFRYSK RRDFKYSLKN
NLTFKRLYSD EDIVCFFNLL SNCLDSKGAK VIHSIEELLD FKNNRLKDIV EFYAVYIDGI
MICGSMVFNF QERVYHTQYL ASNSTYNKYY PMIFLYYNLI KNALERNFKY LSFGISTLNR
GKYLDEGLAT FKEGFGSSAI CNRTYYKNIN K
//