ID A0A316FXV0_9GAMM Unreviewed; 488 AA.
AC A0A316FXV0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=C8D97_103245 {ECO:0000313|EMBL:PWK53418.1};
OS Pleionea mediterranea.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Pleioneaceae; Pleionea.
OX NCBI_TaxID=523701 {ECO:0000313|EMBL:PWK53418.1, ECO:0000313|Proteomes:UP000245790};
RN [1] {ECO:0000313|EMBL:PWK53418.1, ECO:0000313|Proteomes:UP000245790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25350 {ECO:0000313|EMBL:PWK53418.1,
RC ECO:0000313|Proteomes:UP000245790};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWK53418.1}.
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DR EMBL; QGGU01000003; PWK53418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316FXV0; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000245790; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000245790};
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 DOMAIN 80..262
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 140
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 208
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 488 AA; 54295 MW; 851106EFB76DC795 CRC64;
MRQPKTLNAL IPQITSLLTS VVIFGSTAFA ASNQLPDMGS STSRTLSIQQ EQAIGDEYIL
GVRRYLPLAN DPLAVDYINH IGFRLVEQNP EAQDRKFYFF LVKDATLNAF ALPGGYIGTH
TGLVTAAENE SELAAVLGHE IAHVTQRHLA RRLELQNQLS FPALASFIGG IIVASQNPEA
GIGMMATAQA GVKQALINHT RENEKEADRV GIHAMSRAGF DPEAVAAFFE KMQQATRYLR
KPPEFLMTHP VSQTRISDAR ARARSMPAPY DPDSLDFHLI KSRLGVSTEK INSSKYQENA
KRYQNDKVTQ EVELYEFALQ STLNESYNTA ISILTQLYLK RQRNLIYLVS LADAYIAAGQ
PAKAMPFLEA ELKTTPTSYP LIMTYARALI DNEQPRAARA ILLEHAYSGR TEPQIFQLLG
EAQSLSGFVD EVHESQGQYL YATGDLEGAL AQFELAIGRS SDDPYASTRI QAKIDKIRFI
LRQRKTRH
//
