ID A0A0A0JLZ4_9MICO Unreviewed; 408 AA.
AC A0A0A0JLZ4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lipid II:glycine glycyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=N803_03680 {ECO:0000313|EMBL:KGN36661.1};
OS Knoellia subterranea KCTC 19937.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Knoellia.
OX NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN36661.1, ECO:0000313|Proteomes:UP000030011};
RN [1] {ECO:0000313|EMBL:KGN36661.1, ECO:0000313|Proteomes:UP000030011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN36661.1,
RC ECO:0000313|Proteomes:UP000030011};
RA Zhu W., Wang G.;
RT "The genome sequence of Knoellia subterranea.";
RL Submitted (AUG-2013) 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:KGN36661.1}.
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DR EMBL; AVPK01000009; KGN36661.1; -; Genomic_DNA.
DR RefSeq; WP_035906406.1; NZ_AVPK01000009.1.
DR AlphaFoldDB; A0A0A0JLZ4; -.
DR STRING; 1385521.N803_03680; -.
DR eggNOG; COG2348; Bacteria.
DR OrthoDB; 9793335at2; -.
DR Proteomes; UP000030011; 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; 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); 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000030011}.
FT COILED 246..299
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 408 AA; 45294 MW; 7A7630452DA8319D CRC64;
MALAALDLTD REHDDFVRDH PNGHLMQTTP WGREKEHTGW TWRTVAVGRK GAGPDGTDEI
AGAALILFRR TPVLPMALAY CPRGFVVDWA DGEAVDALLA EVTKVAKANR GVLLRIDPAV
RIDNPDIRPA LESRGFTRTD PGDDAAKTLA QPALRMVTDI GDLDQLHKDL SQGTRQSIRK
GEKSGLVYES AGREGVDAFY ELMRITGERD GFGIRSKDYF TTLVDVLSPT DDIVISLVKL
DHGAAADKAR AAVADTRGQL EKAQAKREKY PSDKADRQVS QLEEQIAAKE KSIAEFDAEH
AKHPDGQYLA GSVFATCGTR GSYLYAASSN EHRNLRPNYL MVWRIMQDAA AKGVKTFDFG
GIDASEGLEE FKRQWNPERR EYAGEFTKRV RPLSGRLIDL VVKIYKRR
//
