ID A0A402BSL9_9FIRM Unreviewed; 332 AA.
AC A0A402BSL9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Beta-barrel assembly-enhancing protease {ECO:0000313|EMBL:GCE34321.1};
GN Name=bepA_2 {ECO:0000313|EMBL:GCE34321.1};
GN ORFNames=SPFL3102_02132 {ECO:0000313|EMBL:GCE34321.1};
OS Sporomusaceae bacterium.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae.
OX NCBI_TaxID=1917525 {ECO:0000313|EMBL:GCE34321.1, ECO:0000313|Proteomes:UP000287175};
RN [1] {ECO:0000313|EMBL:GCE34321.1, ECO:0000313|Proteomes:UP000287175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL31 {ECO:0000313|EMBL:GCE34321.1,
RC ECO:0000313|Proteomes:UP000287175};
RA Aoyagi T., Kurasawa H., Amachi S., Nakajima N., Hori T., Yamamura S.;
RT "Draft genome sequence of Sporomusaceae bacterium strain FL31, a lactate-
RT fermenting bacterium of the class Negativicutes.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion
CC inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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:GCE34321.1}.
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DR EMBL; BIFV01000008; GCE34321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402BSL9; -.
DR Proteomes; UP000287175; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07333; M48C_bepA_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00022792};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000287175};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT DOMAIN 44..215
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
SQ SEQUENCE 332 AA; 36732 MW; 887E94B11A603ADE CRC64;
MLAINVLGMP TASAGLISTK EEISIGRDVG KQLEEKYGLV DDPELQARVN RIGMSMVAVS
DRRDLPYSFK VLNSKEINAM AAPGGFIYIF QGLIDLMPSD DELAGVIGHE IGHVVKKHSV
RQMEKSLGIG ILFGVAFGDR GAMLQNLAFN AIMAGHSRSD EREADYLGFS HSFKAGYNPY
SMLLGLYKLS ELDQKYHYDL FSDHPEGKAR VALAQKYLKD AKITPQVAQS EDGKSAYVVD
GTWKLPPIYA SLSGYKPVHR ACFVAGTLYR VKALPDYSPD RYILDTDGTN YTVYYEDRSI
ITITPEDAGA QGLSTQDLAN LYIDALRHWK TK
//
