ID A0A0Q9EKC7_9GAMM Unreviewed; 546 AA.
AC A0A0Q9EKC7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=ASE45_12120 {ECO:0000313|EMBL:KRD67511.1};
OS Lysobacter sp. Root96.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD67511.1, ECO:0000313|Proteomes:UP000050805};
RN [1] {ECO:0000313|EMBL:KRD67511.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD67511.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD67511.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD67511.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRD67511.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMJN01000003; KRD67511.1; -; Genomic_DNA.
DR RefSeq; WP_056305740.1; NZ_LMJN01000003.1.
DR AlphaFoldDB; A0A0Q9EKC7; -.
DR STRING; 1736612.ASE45_12120; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000050805; 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 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:UP000050805};
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..22
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT CHAIN 23..546
FT /note="Putative beta-barrel assembly-enhancing protease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT /id="PRO_5008994930"
FT DOMAIN 67..263
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 131
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 204
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 546 AA; 59379 MW; D2A7D7E33408E025 CRC64;
MRRIALLSAA ITLAVASVCA PAQESSLPDI GSSAGELLTP AQEREYGAMM LAQLRHYDYL
LEDPLINSWL DTLGTRLAAS SDRPRQPFTF FVMRQRQINA FATLGGYIGV NVGLVLAAER
EDEVAAVLSH EIAHVTQQHV LRGVERAQRD QLPILLAMLG AIVAAQAAGG NSADAAAQAA
MVSAMGLMQQ RQIDYTRSNE SEADRLGIQT LARSQYDPAA MADFFAKMQA KSRSNAAGYY
GPTPDYLLTH PVTTTRISEA KARAEQIARS TVVATTTTPN ATRNERIPKN GYSLPGDARG
LDNPLLPGTL KLQGYELSGG ETGFFEFARE RMRVLSAESP RDAIAEYERL GKGKLDDAQR
YGLAVARMRA NQAAAAAPVF AELLQEHPDH LWLSLALSEA ESLSGKAVSA DARFDSLLRQ
MPNNRAVALT YARSLSERNT VEAGKRAQAV LRPLLGAASE DAVFQQVFAR ACEIAGDPIR
AGEAYAEAAY LGGRPEQALV QLNTLKKRPE LDYYSRARIE ARIAAITPTV LELRRQGVKD
EDLRRR
//
