ID A0A139SSH3_9GAMM Unreviewed; 471 AA.
AC A0A139SSH3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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};
GN ORFNames=AXE65_03060 {ECO:0000313|EMBL:KXU37507.1};
OS Ventosimonas gracilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Ventosimonadaceae; Ventosimonas.
OX NCBI_TaxID=1680762 {ECO:0000313|EMBL:KXU37507.1, ECO:0000313|Proteomes:UP000072660};
RN [1] {ECO:0000313|EMBL:KXU37507.1, ECO:0000313|Proteomes:UP000072660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV58 {ECO:0000313|EMBL:KXU37507.1,
RC ECO:0000313|Proteomes:UP000072660};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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}.
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:KXU37507.1}.
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DR EMBL; LSZO01000163; KXU37507.1; -; Genomic_DNA.
DR RefSeq; WP_068390727.1; NZ_LSZO01000163.1.
DR AlphaFoldDB; A0A139SSH3; -.
DR Proteomes; UP000072660; 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 CDD; cd07324; M48C_Oma1-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; 2.
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:UP000072660};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..471
FT /note="Putative beta-barrel assembly-enhancing protease"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012227077"
FT DOMAIN 61..242
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 122
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 191
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 471 AA; 52445 MW; 82B86BA1E17E7C34 CRC64;
MLFVLLLVYP AALLAGDLPS LGDASSGIVS PQQERQLGHA WLSLLRGQVK QLHDSLLKDF
VESSVYRLAE TSALQDRRLS FIFIDSPQLN AFAAPGGLVG VNGGIFITAQ TEAEYASVMA
HELAHLSQRH FARRLQAEQR MQIPMLAALL AGVVAAAAGA GDLGMATIVS SQAAAFQEQM
RFSRQNEQEA DRFGLLNLER AGYDPRAMPA MFGRLLRQYR YASRPPEFLL THPLTENRIA
DTLSRAEQYP PQGKQDSLAY QLVRTRMQLY YEETPGISLK RFTATLSEQP DNQAARYGLA
LSLAKNQQIE EASKALAPLL QQQPENIAFN LAQIELDMAA NRLDMAEKRL TPLLASFPDN
YPLKQAQADL LLKQQKPALA EKVLDELLKT RSNDPDIWYQ SAEAHGLAGN ISALHQARAE
YFALTGDYQQ ALEQIELAKR RAGTNFLLAS RIEARQNELR ELQKTVKEMM R
//
