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Database: UniProt
Entry: A0A0L6Z7X8_9CLOT
LinkDB: A0A0L6Z7X8_9CLOT
Original site: A0A0L6Z7X8_9CLOT 
ID   A0A0L6Z7X8_9CLOT        Unreviewed;       736 AA.
AC   A0A0L6Z7X8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Lactococcin-G-processing and transport ATP-binding protein LagD {ECO:0000313|EMBL:KOA19070.1};
DE            EC=3.4.22.- {ECO:0000313|EMBL:KOA19070.1};
GN   Name=lagD_2 {ECO:0000313|EMBL:KOA19070.1};
GN   ORFNames=CLHOM_25730 {ECO:0000313|EMBL:KOA19070.1};
OS   Clostridium homopropionicum DSM 5847.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121318 {ECO:0000313|EMBL:KOA19070.1, ECO:0000313|Proteomes:UP000037043};
RN   [1] {ECO:0000313|Proteomes:UP000037043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5847 {ECO:0000313|Proteomes:UP000037043};
RA   Poehlein A., Beck M., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA   Duerre P.;
RT   "Genome sequence of the strict anaerobe Clostridium homopropionicum LuHBu1
RT   (DSM 5847T).";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KOA19070.1}.
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DR   EMBL; LHUR01000029; KOA19070.1; -; Genomic_DNA.
DR   RefSeq; WP_052222064.1; NZ_LHUR01000029.1.
DR   AlphaFoldDB; A0A0L6Z7X8; -.
DR   STRING; 36844.SAMN04488501_12914; -.
DR   PATRIC; fig|1121318.3.peg.2583; -.
DR   Proteomes; UP000037043; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043214; F:ABC-type bacteriocin transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd18570; ABC_6TM_PCAT1_LagD_like; 1.
DR   CDD; cd02418; Peptidase_C39B; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005897; Pept_C39_ABC_bacteriocin.
DR   InterPro; IPR005074; Peptidase_C39.
DR   InterPro; IPR039421; Type_1_exporter.
DR   NCBIfam; TIGR01193; bacteriocin_ABC; 1.
DR   PANTHER; PTHR24221:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 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; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KOA19070.1};
KW   Hydrolase {ECO:0000313|EMBL:KOA19070.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protease {ECO:0000256|ARBA:ARBA00022807};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037043};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        167..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        306..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..138
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000259|PROSITE:PS50990"
FT   DOMAIN          171..450
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          485..719
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   736 AA;  82022 MW;  2EFF20DF03F7EF65 CRC64;
     MKNPFKKYTC IKQHDLKDCG AACLATISKQ YGLSIPISKI REVAGTDKLG TSAYGVIKAA
     ESLGFTAKGV KASKPDDIFS QFPLPAIAHV VMEGNLLHYV VIHRINKEEL LIADPGKGIV
     KYKPEDFFKI WTGVLILLVP SAKFKKGDET KGLFSRFLGL LKPQKGLLIN IFFTSLIFTL
     LGILGSFYFK VLVDDILQYS LKKTLHILSI GVIALNIFKI LLNAFRTQLL MYLAQKIDIP
     LMLGYYEHVI GLPMNFFGTR KVGEIVSRFN DATKIREAIS GATLSIMIDT LMAIAGAVIL
     YTQNHLLFGI TLIPVVLYAI IVFSFNKAIK DVNRETMEDN SKITSYLVES LNGIETIKAF
     NAEREVNFET EKRFIKLIKS VFKNGLINNV QASIKGTVKS IFGIAILWIG AYECMEGRLS
     VGELLAFNSL LAYFLDPIEN LINLQTQLQT AIVAADRLGE ILDLGLEKAP NEDKKIKPSS
     LVGQIEFKNV DFRYGTRQLI LENISLSIAP GEKLALVGES GSGKTTLSKL LMNYYQCEKG
     EVLINGYNVK DINIEILRDK IACISQDIFL FSGTITENLS LGNPSLELEA IIEACKKAKI
     HDFINSLPLR YDTLVEENGS NFSGGQKQRL AIARAILRTP EILIMDEATS SLDSITEKAI
     EKTMYDLSKN ITTIIIAHRL STIMRCDKIC VLEKGKIVEY GTHNSLMKEQ GRYFQLWRDQ
     LPDNYEAVSA KEVILA
//
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