ID A0A1I0EIN6_9GAMM Unreviewed; 478 AA.
AC A0A1I0EIN6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Beta-barrel assembly-enhancing protease {ECO:0000256|HAMAP-Rule:MF_00997};
DE EC=3.4.-.- {ECO:0000256|HAMAP-Rule:MF_00997};
DE Flags: Precursor;
GN Name=bepA {ECO:0000256|HAMAP-Rule:MF_00997};
GN ORFNames=SAMN02583745_02389 {ECO:0000313|EMBL:SET44825.1};
OS Thorsellia anophelis DSM 18579.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Thorselliaceae; Thorsellia.
OX NCBI_TaxID=1123402 {ECO:0000313|EMBL:SET44825.1, ECO:0000313|Proteomes:UP000242642};
RN [1] {ECO:0000313|Proteomes:UP000242642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18579 {ECO:0000313|Proteomes:UP000242642};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as both a chaperone and a metalloprotease.
CC Maintains the integrity of the outer membrane by promoting either the
CC assembly or the elimination of outer membrane proteins, depending on
CC their folding state. {ECO:0000256|HAMAP-Rule:MF_00997}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00997};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00997};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_00997}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. BepA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00997}.
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DR EMBL; FOHV01000027; SET44825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0EIN6; -.
DR STRING; 1123402.SAMN02583745_02389; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000242642; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR HAMAP; MF_00997; Protease_BepA; 1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR030873; Protease_BepA.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00997};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00997};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_00997};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_00997};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00997};
KW Reference proteome {ECO:0000313|Proteomes:UP000242642};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00997};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00997}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT CHAIN 22..478
FT /note="Beta-barrel assembly-enhancing protease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT /id="PRO_5017490742"
FT DOMAIN 66..251
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 129
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 478 AA; 52677 MW; EEECB0697D60A499 CRC64;
MKKISVAVLI TMMFSSLPSI ANNTLPDIGT SASTTLSVAQ ENEMGDFYIR AIRGSTPLIN
DPVLNVYINS LGNSLAKYAD GGNQIFNFHL VNNDEINAYA FFGGHVVFHS GLFREVTDEN
ELASVVAHEI AHITQRHLAR AMEAQKKQSP LTWAGVLGGA LLTMANPNAG MAAVTGSLAS
SQQSAISFTQ SNEREADNIG LNIMQRAGFD ARGMNNFMQK MADNARHSSK PPQMLLTHPL
PDSRLADARS RTYQLTEKAR PSSMDFYFAK AKVLALYGNK NGNNTFAFDA LLKGNQYSIN
AHTYGSALKQ MEKRQYAKAF ELLSPLYESM PDNIWLIDAM TDIDLGQGQA TRAITRLEVA
LTKPLFKNNP VIEINLANSY ISVGQFAKAN RLLFNITRRN PNDVNAWYLL AESAAKLGDR
AQELSARAES YALGANIEGA IGLLKQAVTY TDNNQEKAKL NARLKQFEAL KLRFENYR
//
