ID A0A1E8F1B8_9CLOT Unreviewed; 283 AA.
AC A0A1E8F1B8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Stage IV sporulation protein FB {ECO:0000313|EMBL:OFI07220.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:OFI07220.1};
GN Name=spoIVFB {ECO:0000313|EMBL:OFI07220.1};
GN ORFNames=CLOACE_04110 {ECO:0000313|EMBL:OFI07220.1};
OS Clostridium acetireducens DSM 10703.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI07220.1, ECO:0000313|Proteomes:UP000175744};
RN [1] {ECO:0000313|EMBL:OFI07220.1, ECO:0000313|Proteomes:UP000175744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI07220.1,
RC ECO:0000313|Proteomes:UP000175744};
RA Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium acetireducens DSM 10703.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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:OFI07220.1}.
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DR EMBL; LZFO01000004; OFI07220.1; -; Genomic_DNA.
DR RefSeq; WP_070109382.1; NZ_LZFO01000004.1.
DR AlphaFoldDB; A0A1E8F1B8; -.
DR STRING; 1121290.CLAOCE_04110; -.
DR PATRIC; fig|1121290.3.peg.417; -.
DR OrthoDB; 166377at2; -.
DR Proteomes; UP000175744; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd06161; S2P-M50_SpoIVFB; 1.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OFI07220.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000175744};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..96
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 103..157
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 283 AA; 32788 MW; 5A47B26E62703BE9 CRC64;
MIKVNKYFIP YILILLILGF KGEIFLDFLI VIFHEIVHYI TARYYGFSGF AIEILPVGAV
LKLKDLEEAS VKEDLIISLS GPVANLILAL IFYVLNFKIP SLIFEALFIG NATIGLFNLI
PAFPLDGGRI IRDILCTKFL YKKANEITVY ISIIIASFMM FFFIFLFFVN KVNLNIGLVS
LIMIIFSLKE KERIVYIIMG DIIKKKYKFL KRGYLENKYM SIYYKTKLLD ILGMLDKSKY
GIFTVLDNNM KVMDIIYEEE VIEALKLYGN ISVEKFIKIE NRL
//
