LCNC_LACLL
ID LCNC_LACLL Reviewed; 715 AA.
AC Q00564;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lactococcin-A transport/processing ATP-binding protein LcnC;
DE EC=3.4.22.-;
DE EC=7.-.-.-;
GN Name=lcnC;
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG Plasmid pNP2.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Biovar diacetylactis WM4;
RX PubMed=1622271; DOI=10.1128/aem.58.6.1952-1961.1992;
RA Stoddard G.W., Petzel J.P., van Belkum M.J., Kok J., McKay L.L.;
RT "Molecular analyses of the lactococcin A gene cluster from Lactococcus
RT lactis subsp. lactis biovar diacetylactis WM4.";
RL Appl. Environ. Microbiol. 58:1952-1961(1992).
CC -!- FUNCTION: Involved in the export process of the bacteriocin lactococcin
CC A.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Bacteriocin
CC (lactococcin) exporter (TC 3.A.1.112.3) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M90969; AAA92852.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M90969; AAA92854.1; ALT_INIT; Genomic_DNA.
DR PIR; B43943; B43943.
DR AlphaFoldDB; Q00564; -.
DR SMR; Q00564; -.
DR MEROPS; C39.001; -.
DR TCDB; 3.A.1.112.3; 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: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: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 3: Inferred from homology;
KW ATP-binding; Bacteriocin transport; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Plasmid; Protease; Protein transport; Thiol protease;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..715
FT /note="Lactococcin-A transport/processing ATP-binding
FT protein LcnC"
FT /id="PRO_0000092399"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 11..138
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 168..450
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 482..715
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT ACT_SITE 17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT BINDING 515..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 715 AA; 79810 MW; EF3717ECB0F5B0C4 CRC64;
MKFKKKNYTS QVDEMDCGCA ALSMILKSYG TEKSLASLRL LAGTTIEGTS ALGIKKAAEI
LEFSVQALRT DASLFEMKNA PYPFIAHVIK DQKYPHYYVI TGANKNSVFI ADPDPTIKMT
KLSKEAFLSE WTGISLFLST TPSYHPTKEK ASSLLSFIPI ITRQKKVILN IVIASFIVTL
INILGSYYLQ SMIDSYIPNA LMGTLGIISV GLLLTYIIQQ VLEFAKAFLL NVLSQRLAID
VILSYIRHIF QLPMSFFSTR RTGEITSRFS DASSILDAIA STILSLFLDL TIVVMTGLIL
GLQNMQLFLL VLLAIPLYIV VIIIFTPLFE KQNHEVMQTN AVLNSSIIED INGIETIKAL
ASEQERYQKI DYEFASYLKK AFTLQKSEAI QGLIKAIIQL TLSVTILWFG ATLVISQKIT
LGQLITFNAL LSYFTNPITN IINLQTKLQK ARVANERLNE VYLVPSEFEE KKTELSLSHF
NLNMSDISYQ YGFGRKVLSE IELSIKENEK LTIVGMSGSG KSTLVKLLVN FFQPTSGTIT
LGGIDLQQFD KHQLRRLINY LPQQPYIFTG SILDNLLLGA NENASQEEIL KAVELAEIRA
DIEQMQLGYQ TELSSDASSL SGGQKQRIAL ARALLSPAKI LILDEATSNL DMITEKKILK
NLLPLDKTII FIAHRLSVAE MSHRIIVVDQ GKVIESGSHV DLLAQNGFYE QLYHN
