LAGD_LACLL
ID LAGD_LACLL Reviewed; 703 AA.
AC P59852;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Lactococcin-G-processing and transport ATP-binding protein LagD;
DE EC=3.4.22.-;
DE EC=7.-.-.-;
GN Name=lagD;
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], IDENTIFICATION OF PROTEOLYTIC ACTIVITY,
RP AND MUTAGENESIS.
RC STRAIN=LMG 2081;
RX PubMed=7565085; DOI=10.1111/j.1365-2958.1995.tb02295.x;
RA Havarstein L.S., Diep D.B., Nes I.F.;
RT "A family of bacteriocin ABC transporters carry out proteolytic processing
RT of their substrates concomitant with export.";
RL Mol. Microbiol. 16:229-240(1995).
CC -!- FUNCTION: LagD (TC 3.A.1) is involved in processing the signal peptide
CC and probably also in export of the bacteriocin lactococcin G.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The first 150 amino acids are capable of cleaving the signal
CC sequence of LagA, the lactococcin G alpha precursor.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. LagD family.
CC {ECO:0000305}.
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DR AlphaFoldDB; P59852; -.
DR SMR; P59852; -.
DR MEROPS; C39.001; -.
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:0043214; F:ABC-type bacteriocin 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:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR005897; Pept_C39_ABC_bacteriocin.
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 TIGRFAMs; TIGR01193; bacteriocin_ABC; 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 1: Evidence at protein level;
KW Antibiotic biosynthesis; ATP-binding; Bacteriocin transport; Cell membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Protease; Protein transport;
KW Thiol protease; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..703
FT /note="Lactococcin-G-processing and transport ATP-binding
FT protein LagD"
FT /id="PRO_0000092397"
FT TRANSMEM 162..182
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 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 7..132
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 153..435
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 469..703
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 13
FT BINDING 502..509
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 13
FT /note="C->A: Complete loss of precursor processing."
FT /evidence="ECO:0000269|PubMed:7565085"
FT MUTAGEN 95
FT /note="V->M: 5-fold reduction of precursor processing."
FT /evidence="ECO:0000269|PubMed:7565085"
SQ SEQUENCE 703 AA; 79350 MW; 138FFEE416E81873 CRC64;
MKKIIYQQDE KDCGVACIAM ILKHYGTEIT IQRLRELSGT DLDGTSAFGI KKTFEKLGFD
APAFKAGDET WQEKDIPLPL IAHIISEQKY QHYVVVYKVK GDEIWIADPA KGKIRKTISE
FSKEWTGVLL FPKPKAEYKP SIERVDSLST FFPILIKQKS LFITIFGIIS SYYFQGLLDN
IIPNQARSTL NILSIGLIFV YLFRVLFEYS RSYLLLLIGQ RMSMSIMLGY FKHVLSLPLS
FFATRKSGEI ISRFLDANKI IDALASATLS LILDIGMVIL VGTTLAIQST QLFLLTLAFL
PFYILVVYVF IRSYDKANTE EMSAGAEVNS SIIESLKGIE TIKSYNGENH VYDRVDSEFV
TLMKKSFKSV TLDNVQQSLK MVIELISSVL ILWLGSSYVI DGKISLGQLI TYNALLVFFT
EPLQNIINLQ VKMQKARVAN KRLNEIMSIS PEQRNTNINI SKNIFNKDIK LDKVSFSYNM
KLPVLRDVSL EIYSKSKVAL VGVSGSGKST LAKLLVKFYD PSEGNITYGD INCQDIENHK
LRNHVTYVPQ ESFFFNGTII DNLTFGLSHQ PEFEKIFRAC KAACLVDFIN QQPLRFDSVL
EEGGNNLSGG QKQRLAIARA ILNDSEIIIF DEATSGLDTL LEKEILEYLI KLQDKTIIFI
AHHLSIAKAC DEIIVLDQGI LVGRGTHEEL SEKEGVYRRL LNA
