ID Q65GL0_BACLD Unreviewed; 249 AA.
AC Q65GL0; Q62S18;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=DNA-binding protein {ECO:0000313|EMBL:AAU24442.2};
GN Name=comC {ECO:0000313|EMBL:AAU24442.2};
GN OrderedLocusNames=BL00633 {ECO:0000313|EMBL:AAU24442.2};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU24442.2, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU24442.2, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase A24 family.
CC {ECO:0000256|ARBA:ARBA00005801}.
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DR EMBL; CP000002; AAU24442.2; -; Genomic_DNA.
DR RefSeq; WP_011198164.1; NC_006322.1.
DR AlphaFoldDB; Q65GL0; -.
DR STRING; 279010.BL00633; -.
DR MEROPS; A24.019; -.
DR GeneID; 66215078; -.
DR KEGG; bli:BL00633; -.
DR PATRIC; fig|279010.13.peg.2995; -.
DR eggNOG; COG1989; Bacteria.
DR HOGENOM; CLU_057101_0_1_9; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1220; -; 1.
DR InterPro; IPR000045; Prepilin_IV_endopep_pep.
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.
DR Pfam; PF01478; Peptidase_A24; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000313|EMBL:AAU24442.2};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 71..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..90
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 101..205
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 249 AA; 26955 MW; 40C1D981DFD8F153 CRC64;
MFIFYLFTAG LVLGSFFNSA GRRIPEKISL IAPRSLCRVC KRQLGFSELI PVLSYLMQRG
RCKGCQTPLS IVYPAVELSA AILFAFAGMH VGHEGELVIV LALISLLLIV FVSDVTHMII
PDAVLCFFLP VFAVGRFLVP LEQWHSSLSG AMAGGMLPLL TLLLTKGGIG WGDVKLFAVI
GMALGSRLLV LAFFLSAAAG TVLGLIALLA GKLKKNEPMP FAPAILAGTL TSCFYGEPMI
EWYLQTAWW
//
