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Database: UniProt
Entry: A0A0R1RBR4_9LACO
LinkDB: A0A0R1RBR4_9LACO
Original site: A0A0R1RBR4_9LACO 
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
//
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