ID B6EJT7_ALISL Unreviewed; 484 AA.
AC B6EJT7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Putative 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 OrderedLocusNames=VSAL_I2384 {ECO:0000313|EMBL:CAQ80068.1};
OS Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS LFI1238)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ80068.1, ECO:0000313|Proteomes:UP000001730};
RN [1] {ECO:0000313|EMBL:CAQ80068.1, ECO:0000313|Proteomes:UP000001730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ80068.1,
RC ECO:0000313|Proteomes:UP000001730};
RX PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT LFI1238 shows extensive evidence of gene decay.";
RL BMC Genomics 9:616-616(2008).
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; FM178379; CAQ80068.1; -; Genomic_DNA.
DR RefSeq; WP_012550877.1; NC_011312.1.
DR AlphaFoldDB; B6EJT7; -.
DR MEROPS; M48.023; -.
DR KEGG; vsa:VSAL_I2384; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_0_1_6; -.
DR Proteomes; UP000001730; Chromosome 1.
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 CDD; cd07333; M48C_bepA_like; 1.
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 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..25
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT CHAIN 26..484
FT /note="Putative beta-barrel assembly-enhancing protease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT /id="PRO_5009007877"
FT DOMAIN 71..255
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 135
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 484 AA; 53672 MW; 8C64D5F18497129A CRC64;
MFKLKKLASS LLIASLLTSS LPASANNDLD LPEIGTTAAG TLTIDQELVY GDAYMRMLRA
SQPVINDPVL TEYVQNLGHR LVANASDVKT PFHFFLINNR EINAFAFFGG YVALHSGLFL
YAQSESELAS VVAHEIAHIT QRHLARSMED QARRSPATIA ALVGSLLLAI AAPEAGIAAI
HATTAGAMQS SINYTRSNEK EADRFGIDTL AKSGFDVTAM PRFFSRLADQ YRYASTPPPM
LLTHPLPADR ITDSRARAQQ YPMRRVNTSL RYQLARSRIV ARFAGIDSNA ALDWFSRKSK
SAKVDQKTAI EYGKALVYID SNQYDKATPI MSTLLKNDPL NTFYIDAATD LDLYTKKNEQ
AIKRLENGLI HLPNNPVLMI NYAHALSESG KTPQAVRILQ RYTHDHPKDP TGWQLLSKAY
YDDGSSDGEL AARAEVYALK GMWNKALSNY TQASQLAELG SLDQARYDAR IDQLRLSRER
FSTL
//
