ID A0A0Q7S0F4_9BURK Unreviewed; 349 AA.
AC A0A0Q7S0F4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidoglycan bridge formation protein FemAB {ECO:0000313|EMBL:KQY81410.1};
GN ORFNames=ASD35_06215 {ECO:0000313|EMBL:KQY81410.1};
OS Pelomonas sp. Root1444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=1736464 {ECO:0000313|EMBL:KQY81410.1, ECO:0000313|Proteomes:UP000051648};
RN [1] {ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|Proteomes:UP000051648};
RA Garrido-Oter R., Mueller D.B.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY81410.1, ECO:0000313|Proteomes:UP000051648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1444 {ECO:0000313|EMBL:KQY81410.1,
RC ECO:0000313|Proteomes:UP000051648};
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:KQY81410.1}.
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DR EMBL; LMFP01000028; KQY81410.1; -; Genomic_DNA.
DR RefSeq; WP_056876892.1; NZ_LMFP01000028.1.
DR AlphaFoldDB; A0A0Q7S0F4; -.
DR STRING; 1736464.ASD35_06215; -.
DR OrthoDB; 9773932at2; -.
DR Proteomes; UP000051648; 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; IPR038740; BioF2-like_GNAT_dom.
DR InterPro; IPR003447; FEMABX.
DR InterPro; IPR017469; PEP-CTERM_FemAB-rel.
DR NCBIfam; TIGR03019; pepcterm_femAB; 1.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051648}.
FT DOMAIN 159..281
FT /note="BioF2-like acetyltransferase"
FT /evidence="ECO:0000259|Pfam:PF13480"
SQ SEQUENCE 349 AA; 39517 MW; F910C75D88D3EE32 CRC64;
MTSPLRIARL AAQDQALSAR WDAFVLAHPQ ATFFHRSGWL RVIERSFGHR GFFLYAERDG
VIEGVLPLAE VKSRLFGHSV ASLPFAVYGG VAALNDEAAA ALEVEAEKIA RGQGAEHLEY
RNLGATRHAD WPRQDLYVTF RKEILPDEEA NMLAIPRKQR AMVRKGIKNE LKAEVDAGVD
RFFDLYADNV HRHGTPAMPK KYFQALLDEF GADAEVLTVT GPDGKPLSSV LSFYFRDEVL
PYYAGDDEAA RDLAANDFKY WELMRRACAR GLKVFDYGRS KQGTGSFSFK KNWGFEPQPL
SYEYRLFKRD AIPQNNPNNP KYQLLIKTWR KLPIGVANWL GPFIVKNLG
//
