GenomeNet

Database: UniProt
Entry: K2EAZ4_9BACT
LinkDB: K2EAZ4_9BACT
Original site: K2EAZ4_9BACT 
ID   K2EAZ4_9BACT            Unreviewed;       192 AA.
AC   K2EAZ4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Methicillin resistance protein {ECO:0000313|EMBL:EKD95754.1};
DE   Flags: Fragment;
GN   ORFNames=ACD_24C00351G0002 {ECO:0000313|EMBL:EKD95754.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD95754.1};
RN   [1] {ECO:0000313|EMBL:EKD95754.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD95754.1}.
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; AMFJ01010292; EKD95754.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2EAZ4; -.
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; IPR038740; BioF2-like_GNAT_dom.
DR   InterPro; IPR003447; FEMABX.
DR   PANTHER; PTHR36174; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   PANTHER; PTHR36174:SF1; LIPID II:GLYCINE GLYCYLTRANSFERASE; 1.
DR   Pfam; PF13480; Acetyltransf_6; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
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}.
FT   DOMAIN          16..142
FT                   /note="BioF2-like acetyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF13480"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EKD95754.1"
SQ   SEQUENCE   192 AA;  22111 MW;  ECBA3C4E083C930B CRC64;
     KSEEEMWSEF SHSAKYSITR AIREGYRAVK ISKPSISQLE ESYALLSVTA RKKNFYVSPI
     REFSTRVESF GDRSYLCEVR DKDGILQSSK FCLGHKNMVL FVAGGSSESA RKNKSGYLLM
     WEAMKFLKSE GYEVFDLEGK DDPRFPFQTR NWEGFSHFKE KFGGVAIEFP VPRIKFLNKI
     YGTVSRITGV DF
//
DBGET integrated database retrieval system