ID   R7NH74_9MOLU            Unreviewed;       413 AA.
AC   R7NH74;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=tRNA-dependent lipid II--L-alanine ligase {ECO:0000313|EMBL:CDF12115.1};
GN   ORFNames=BN778_01161 {ECO:0000313|EMBL:CDF12115.1};
OS   Mycoplasma sp. CAG:776.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1262906 {ECO:0000313|EMBL:CDF12115.1, ECO:0000313|Proteomes:UP000018174};
RN   [1] {ECO:0000313|EMBL:CDF12115.1, ECO:0000313|Proteomes:UP000018174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:776 {ECO:0000313|Proteomes:UP000018174};
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:CDF12115.1}.
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DR   EMBL; CBKH010000033; CDF12115.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7NH74; -.
DR   STRING; 1262906.BN778_01161; -.
DR   Proteomes; UP000018174; 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; 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   Ligase {ECO:0000313|EMBL:CDF12115.1};
KW   Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018174}.
SQ   SEQUENCE   413 AA;  48906 MW;  2FD71FD4338567BB CRC64;
     MHIKELSIAE FDTFAQNFPI SSYYQSSNYA LFMAELGYDY ELIGFVDELG IIKAASLILI
     KKIGLSSKYG YSPKGFLVDY FDLDLLKKFT EAIRDYYSKK LAFIKINPEI AIGEIDIRTK
     LTNYNQNIII RDYLKELGYL KLKDNKYFES LFPRFNGILN LREYSFSSLE KNTKNKIRKA
     IKKGLVFEKA DRNSLDILFQ FIKKKKDIDP FYYKNYFNVF ARIGAADLFL IKIDYQQYLV
     NSKRLYDQEF ERNQEISHKL IQHSSDIYIK EKMNSDKILL TYKNDIEIAT KGLRENRNDY
     IAGAFVIRYL NRIHIAISGY DKAFKHFDPN YFLHYNILEF YKDQFKFVDL NGMTGDFTIS
     NPYKGLNQFK LGFKPHIYEF IGEFDLILNE RVYRTLIKKG LLAKEFNKKT KEI
//