ID   R6IAB2_9FIRM            Unreviewed;       405 AA.
AC   R6IAB2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=tRNA-dependent lipid II--L-alanine ligase {ECO:0000313|EMBL:CDB42381.1};
GN   ORFNames=BN517_00606 {ECO:0000313|EMBL:CDB42381.1};
OS   Ruminococcus sp. CAG:177.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=1262952 {ECO:0000313|EMBL:CDB42381.1, ECO:0000313|Proteomes:UP000018315};
RN   [1] {ECO:0000313|EMBL:CDB42381.1, ECO:0000313|Proteomes:UP000018315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:177 {ECO:0000313|Proteomes:UP000018315};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDB42381.1}.
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DR   EMBL; CBDQ010000119; CDB42381.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6IAB2; -.
DR   STRING; 1262952.BN517_00606; -.
DR   Proteomes; UP000018315; 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: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; -; 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   Ligase {ECO:0000313|EMBL:CDB42381.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018315}.
SQ   SEQUENCE   405 AA;  45842 MW;  71D7F80D9B0007BF CRC64;
     MAEYNFKTGV DAGEYRDFLN VSPAYCFTQL PEWSEVKDNW DHDICMLYKD GAPEVGALLL
     IRHLPMGKKL IYSPRGPVGD FGDAEAMREF STQLKKYAKK IGAIAVKADP FVIRENYEKQ
     NAADFGNSFD ETIRVMQECG FVHRGLSTDI NAYFQPRFNM AIPLFNENGP IDSAGFLKAV
     PKKTRYYMGS FHNSKGIEFI KADPDDDLSE FVRLLGQTEK RQGISLRNEE YFKKIRHAFG
     DRAVIYYARM HLDRYVEYLE GLIAKKQNIP ENTRKLDEAK ALIEEKGNTV NLAASLVIMP
     DPQAKLKIAE YLYAGSDLSV LSTLCASVGL IYAGVCDSID AGCDYFNLGG VDGSFEDHLS
     KFKIKFVPHI FEYVGEFDMP VDKVMYLGFE KLLPMAKKAI KKIKK
//