ID   LCN3_LACLL              Reviewed;         691 AA.
AC   P37608;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Lacticin-481/lactococcin-DR transport/processing ATP-binding protein lcnDR3;
DE            EC=3.4.22.-;
DE            EC=7.-.-.-;
GN   Name=lcnDR3;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ADRIA 85LO30;
RX   PubMed=8017945; DOI=10.1128/aem.60.5.1652-1657.1994;
RA   Rince A., Dufour A., le Pogam S., Thuault D., Bourgeois C.M., Pennec J.P.;
RT   "Cloning, expression, and nucleotide sequence of genes involved in
RT   production of lactococcin DR, a bacteriocin from Lactococcus lactis subsp.
RT   lactis.";
RL   Appl. Environ. Microbiol. 60:1652-1657(1994).
CC   -!- FUNCTION: Probably implicated in the export process of the lantibiotic
CC       lacticin-481/lactococcin-DR.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; U91581; AAC72259.1; -; Genomic_DNA.
DR   AlphaFoldDB; P37608; -.
DR   SMR; P37608; -.
DR   MEROPS; C39.007; -.
DR   TCDB; 3.A.1.111.5; the atp-binding cassette (abc) superfamily.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02425; Peptidase_C39F; 1.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR033839; Lacticin_481_peptidase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; PTHR24221; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF03412; Peptidase_C39; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS50990; PEPTIDASE_C39; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Bacteriocin transport; Cell membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Protease; Protein transport; Thiol protease;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..691
FT                   /note="Lacticin-481/lactococcin-DR transport/processing
FT                   ATP-binding protein lcnDR3"
FT                   /id="PRO_0000092400"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        262..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        289..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          6..130
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   DOMAIN          158..434
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          464..689
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   ACT_SITE        12
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   BINDING         497..504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   691 AA;  79834 MW;  4276DD778AEC0B47 CRC64;
     MKIVLQNNEQ DCLLACYSMI LGYFGRDVAI HELYSGEMIP PDGLSVSYLK NINMKHQVSM
     HVYKTDKKNS PNKIFYPKML PVIIQWNDNH FVVVTKIYRK NVTLIDPAIG KVKYNYNDFM
     KKFSGYIITL SPNSSFTKKK RISEIIFPLK KIFKNRNTFL YIFSLFISQI VALWFSIILR
     DILNKSHDIT YSFIMMISLV LFQTLSLLMK LGAQKNTNLL YESKISRQIF KGIFSRPLLY
     FRNNSVGTII EKINLRTGIR DGILLKIFPS LLNFFTVFIV IIYLGTISFT LTLFLVIMNL
     LYMIFSFSLI SIKRQANIQY TQQTIDFTSV VQEDLNQIEQ IKAQANEKEC VKRWTKKSAQ
     TIFSYNKILN IDGITSAFNQ GFNYICVILM MIFGIYLNQG NLVSIPDLII FQSGISLFVS
     AVNQIQDVMF EISRLSIYGN KISDLLIENP QRIDNIEKHS NNAIILKDIS YSYELNNYIF
     NNINFSIKKG EKIAIVGKSG SGKSTLFNIL LGLISYEGEV TYGYENLRQI IGVVSQNMNL
     RKGSLIENIV SNNNSEELDI QKINDVLKDV NMLELVDSLP QKIFSQLFEN GKNLSGGQIQ
     RLLIAKSLLN NNKFIFWDEP FSSLDNQNRI HIYKNVLENP DYKSQTIIMI SHHLDVLKYV
     DRVIYIDDKK IMIDKHNNLL LNDSYNSFVN E