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Database: UniProt
Entry: S6F1G2_LACLL
LinkDB: S6F1G2_LACLL
Original site: S6F1G2_LACLL 
ID   S6F1G2_LACLL            Unreviewed;       221 AA.
AC   S6F1G2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Aspartic endopeptidase, MEROPS family A24 (Type IV prepilin peptidase family) {ECO:0000313|EMBL:CDG05478.1};
DE            EC=3.4.23.43 {ECO:0000313|EMBL:CDG05478.1};
GN   Name=comC {ECO:0000313|EMBL:CDG05478.1};
GN   ORFNames=O9U_06375 {ECO:0000313|EMBL:CDG05478.1};
OS   Lactococcus lactis subsp. lactis A12.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1137134 {ECO:0000313|EMBL:CDG05478.1, ECO:0000313|Proteomes:UP000015361};
RN   [1] {ECO:0000313|EMBL:CDG05478.1, ECO:0000313|Proteomes:UP000015361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A12 {ECO:0000313|EMBL:CDG05478.1,
RC   ECO:0000313|Proteomes:UP000015361};
RX   PubMed=23872564; DOI=10.1128/AEM.01560-13;
RA   Passerini D., Coddeville M., Le Bourgeois P., Loubiere P., Ritzenthaler P.,
RA   Fontagne-Faucher C., Daveran-Mingot M.L., Cocaign-Bousquet M.;
RT   "The Carbohydrate Metabolism Signature of Lactococcus lactis Strain A12
RT   Reveals Its Sourdough Ecosystem Origin.";
RL   Appl. Environ. Microbiol. 79:5844-5852(2013).
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:CDG05478.1}.
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DR   EMBL; CBLU010000020; CDG05478.1; -; Genomic_DNA.
DR   RefSeq; WP_021723103.1; NZ_CBLU010000020.1.
DR   AlphaFoldDB; S6F1G2; -.
DR   Proteomes; UP000015361; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR010627; Prepilin_pept_A24_N.
DR   PANTHER; PTHR30487:SF0; PREPILIN LEADER PEPTIDASE_N-METHYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR30487; TYPE 4 PREPILIN-LIKE PROTEINS LEADER PEPTIDE-PROCESSING ENZYME; 1.
DR   Pfam; PF06750; A24_N_bact; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:CDG05478.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..90
FT                   /note="Prepilin peptidase A24 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06750"
SQ   SEQUENCE   221 AA;  25676 MW;  4E5A3FEB96424104 CRC64;
     MDILFIFVIG SIFGSFFGLI VDRIPLRKSI IFGRSHCDSC QRLLAYRDLI PIFSQLSSGS
     QCRYCKSKIP YLYIFLEFST ALIFVLAWVN YLNPSQFLMI ILSLILSAFD YRQHSFPFVT
     WFIFALSFIL IFPLSPIFYF WLILALLAEK FNLRVGSGDF LWFFTASFSL TFLNEMLLLQ
     IACSLGIIYY LITKKRAEIA FIPFLTIAYL MLLFGHQILS P
//
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