ID   Q927C1_LISIN            Unreviewed;       525 AA.
AC   Q927C1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Lin2868 protein {ECO:0000313|EMBL:CAC98094.1};
GN   OrderedLocusNames=lin2868 {ECO:0000313|EMBL:CAC98094.1};
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626 {ECO:0000313|EMBL:CAC98094.1, ECO:0000313|Proteomes:UP000002513};
RN   [1] {ECO:0000313|EMBL:CAC98094.1, ECO:0000313|Proteomes:UP000002513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262 {ECO:0000313|Proteomes:UP000002513};
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA   Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA   Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA   Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA   Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA   Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
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DR   EMBL; AL596173; CAC98094.1; -; Genomic_DNA.
DR   PIR; AF1790; AF1790.
DR   RefSeq; WP_010991418.1; NC_003212.1.
DR   AlphaFoldDB; Q927C1; -.
DR   STRING; 272626.gene:17567255; -.
DR   KEGG; lin:lin2868; -.
DR   eggNOG; COG0365; Bacteria.
DR   HOGENOM; CLU_000022_59_10_9; -.
DR   OrthoDB; 9778383at2; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0016878; F:acid-thiol ligase activity; IEA:UniProt.
DR   GO; GO:0016405; F:CoA-ligase activity; IEA:UniProt.
DR   CDD; cd05972; MACS_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43605:SF10; ACYL-COA SYNTHETASE MEDIUM CHAIN FAMILY MEMBER 3; 1.
DR   PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598}.
FT   DOMAIN          19..381
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          431..509
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
SQ   SEQUENCE   525 AA;  59323 MW;  E8D29182E916E013 CRC64;
     MNSEKLIAPE LYNITDEIAK FSSEKTALIW KNEHDETKTW SYRHLLEQAN KFANVVKDAG
     VKKGDHVIVM TPRLLETYAI YMGLWKAGAI IIPASELLKA HDLEYRIRHA NVKAIVSYNG
     MTAEFDKIEN IPSVSKKIIV GEKLSGWDHY ETLMETASTE FERVETSRDD ACLLAFTSGT
     TGNPKGVVHI HGWGYAHIRI AADHWLDIHE DDIVWATAGP GWQKWVWSPF LSVLGKGATG
     FIYNGRFIPE KQLHLLEEEK INVLCCTPTE YRLMAKVNNL REHDLSALRS AVSAGEPLNR
     EVIQVFQDNF DIKVRDGYGQ TESTLLIGTL VDTPIRPGSM GKPIMPEYMA IIDAEGTPVG
     VGEIGDIAMR RDFPALFKEY YKEPERLQKA IRGDYFVSGD RAIRDEDNYY WFQGRNDDII
     ISSGYTIGPF EVEDALTHHP AVKEVAVVAS PDEIRGTVVK AFIVLKDGYE GTEDLVHELQ
     TFTKEQTAPY KYPRRIEFVE ALPKTDSGKI RRVELRDAEF ASVHG
//