ID A0A0S9BUI7_9MICC Unreviewed; 330 AA.
AC A0A0S9BUI7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Methicillin resistance protein {ECO:0000313|EMBL:KQN85063.1};
GN ORFNames=ASE96_15990 {ECO:0000313|EMBL:KQN85063.1};
OS Arthrobacter sp. Leaf69.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736232 {ECO:0000313|EMBL:KQN85063.1, ECO:0000313|Proteomes:UP000051467};
RN [1] {ECO:0000313|EMBL:KQN85063.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN85063.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN85063.1, ECO:0000313|Proteomes:UP000051467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf69 {ECO:0000313|EMBL:KQN85063.1,
RC ECO:0000313|Proteomes:UP000051467};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQN85063.1}.
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DR EMBL; LMLR01000015; KQN85063.1; -; Genomic_DNA.
DR RefSeq; WP_056433122.1; NZ_LMLR01000015.1.
DR AlphaFoldDB; A0A0S9BUI7; -.
DR STRING; 1736232.ASE96_15990; -.
DR OrthoDB; 9793335at2; -.
DR Proteomes; UP000051467; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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 CDD; cd04301; NAT_SF; 1.
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 InterPro; IPR000182; GNAT_dom.
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); 2.
DR PROSITE; PS51191; FEMABX; 1.
DR PROSITE; PS51186; GNAT; 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 144..291
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 330 AA; 35768 MW; DBCC135E42A5E094 CRC64;
MDHFLQSPPW AAFQRSLGRT VHQRSGPGWS FLAIEESNPA GKLLYAPYGP VAASLTAFDA
ALAALTDLAR SCGAVFVRIE PVDAGFAAAE ADALLRTRGL RPAPANQQPE LSWIVDVDRD
FKDVLADMKP VNRNLYRNIH KKGVTFRSSQ DPDDISVLLT FLHLTAARNG FKPQSDEYLT
QVARSLMPAG AATLFVAELE GEPIAAALAY DSADTRTYAH AALDDAHRKL SAGIPLLVTL
MADAKAKGLK HVDLWGVAPA DQPDHKWAGF TAFKKSFGGR EVVYPGTWDL PVNKLRYSGY
QLARRGAQAA RRGVRAARTA PARVRGALGR
//
