ID C6PX59_9CLOT Unreviewed; 253 AA.
AC C6PX59;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Peptidase A24A domain protein {ECO:0000313|EMBL:EET86176.1};
GN ORFNames=CcarbDRAFT_3376 {ECO:0000313|EMBL:EET86176.1};
OS Clostridium carboxidivorans P7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536227 {ECO:0000313|EMBL:EET86176.1, ECO:0000313|Proteomes:UP000004198};
RN [1] {ECO:0000313|EMBL:EET86176.1, ECO:0000313|Proteomes:UP000004198}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P7 {ECO:0000313|EMBL:EET86176.1,
RC ECO:0000313|Proteomes:UP000004198};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT "The draft genome of Clostridium carboxidivorans P7.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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:EET86176.1}.
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DR EMBL; ACVI01000062; EET86176.1; -; Genomic_DNA.
DR RefSeq; WP_007062261.1; NZ_GG770677.1.
DR AlphaFoldDB; C6PX59; -.
DR STRING; 536227.Ccar_18505; -.
DR KEGG; cck:Ccar_18505; -.
DR PATRIC; fig|536227.13.peg.3873; -.
DR eggNOG; COG1989; Bacteria.
DR OrthoDB; 9789291at2; -.
DR Proteomes; UP000004198; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000004198};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..93
FT /note="Prepilin peptidase A24 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06750"
FT DOMAIN 105..209
FT /note="Prepilin type IV endopeptidase peptidase"
FT /evidence="ECO:0000259|Pfam:PF01478"
SQ SEQUENCE 253 AA; 28683 MW; D4C92D2CC9169A60 CRC64;
MFILDLIFVM IIGLMIGSFL NVCIYRIPRG ESIAYPPSHC TDCGRKIKWY DLIPIFSYIL
LKGKCRYCCE KISIRYPIIE FVTGILFLLT YLEYGPSIQF VKYVVLIAIL IVVGMIDLNT
TDVYFSTSII GIVFGIIFIL VGAYCHDDFK QYIFGALFGG GVIASIALFT KAMGLGDAEI
CFYSGLFLGI KLTVISIYFS FIFGSIITLL LIILKKKEKK DYIAFGPFIA LASIFTMFLG
NKVLMWYFQN MIY
//
