ID A0A0R1RBR4_9LACO Unreviewed; 432 AA.
AC A0A0R1RBR4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Trna-dependent lipid ii-ala--l-alanine ligase {ECO:0000313|EMBL:KRL54343.1};
GN ORFNames=FD35_GL002683 {ECO:0000313|EMBL:KRL54343.1};
OS Furfurilactobacillus rossiae DSM 15814.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=1114972 {ECO:0000313|EMBL:KRL54343.1, ECO:0000313|Proteomes:UP000051999};
RN [1] {ECO:0000313|EMBL:KRL54343.1, ECO:0000313|Proteomes:UP000051999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15814 {ECO:0000313|EMBL:KRL54343.1,
RC ECO:0000313|Proteomes:UP000051999};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL54343.1}.
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DR EMBL; AZFF01000009; KRL54343.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R1RBR4; -.
DR STRING; 1114972.FD35_GL002683; -.
DR PATRIC; fig|1114972.6.peg.2749; -.
DR eggNOG; COG2348; Bacteria.
DR Proteomes; UP000051999; Unassembled WGS sequence.
DR GO; GO:0016755; F:aminoacyltransferase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IEA:InterPro.
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:SF2; AMINOACYLTRANSFERASE FEMA; 1.
DR PANTHER; PTHR36174; 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}; Ligase {ECO:0000313|EMBL:KRL54343.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Reference proteome {ECO:0000313|Proteomes:UP000051999}.
FT COILED 267..319
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 432 AA; 49797 MW; 3E98CE4D719C1FA8 CRC64;
MVDAFLVSKK WNGVKMVQKV RELSAEEFGA FEEKCPYGSF YQSVEQGNLM LKEGHKATYM
GLVDGDKIIV AGLLVGMKIH FGYRFDIYGG PLFMPGSETK ANLSAFVEAV EEYVRKQNGM
FLRLIPNLPV KTYNDAGELT ASHFETLPAL FKELGYDYQD YHAAGYDEAT HVTHYEYKKD
VRDMTEQTLE KSFDKKARYN IKKAKEFGVK LRDISFDELP EFKKDTAMTA ERLHFPDKSL
DYYQNVYREF GDKIRFVVAE IDSNEYIDSY QQKIKSTDDK IAALKAKNKG YEQNKIDDLE
RQKANHQKKI DVAKDLQKRY PAKFNVAGAM FVIQPQEIDY VFSYTNEEFK TFKGPFMLQD
AMMKAAVDQK IPTYNFLGVA GLFDGSDGVF EFKQGFNGYT DEMIGEFSKV LIPWRYKLLN
AIKTVLGRSK RF
//