ID A0A1H2IH19_9PSED Unreviewed; 477 AA.
AC A0A1H2IH19;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN05216580_3005 {ECO:0000313|EMBL:SDU43402.1};
OS Pseudomonas guangdongensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1245526 {ECO:0000313|EMBL:SDU43402.1, ECO:0000313|Proteomes:UP000243063};
RN [1] {ECO:0000313|Proteomes:UP000243063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC 2012022 {ECO:0000313|Proteomes:UP000243063};
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; LT629780; SDU43402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2IH19; -.
DR STRING; 1245526.SAMN05216580_3005; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000243063; Chromosome i.
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 InterPro; IPR019734; TPR_repeat.
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 SMART; SM00028; TPR; 3.
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:UP000243063};
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..477
FT /note="Putative beta-barrel assembly-enhancing protease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT /id="PRO_5009356343"
FT DOMAIN 67..251
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 128
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 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 131
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 477 AA; 53041 MW; FC7462531CDAE37C CRC64;
MKILRPTLLT LACLLATPLA ASDLPALGDA SSSIVSPDQE YQLGRAWLNL LRGQVKSLPD
PLLMDFIETS VYRLAETSQL DDRRLAFVLL DSAQLNAFAA PGGVIGVNAG LLLHAQNEGE
YASVLAHELA HLSQRHFARG LEEQKRMQVP LMAALLAGVV AAAAGAGDAG IAAIASTQAA
AIQAQRSFSR QNEQEADRIG LLNLQRAGYD PRNMPSMFER LMRQYRYTRV PPEFLLTHPV
NESRVADTRN RAEQFAGNGR SDSLLYQLMR ARVQLHYENT PGLAAKRFRA QLDENPRLDA
ARYGLALAQR RSGQLDEARQ TLQPLLQQAP NDIVYNLAHI ELDIAGDRLT DAEQRLQRLL
GLYPSSYPLR QQQAELLLKQ GRAKEAEKAF DALLAERPND SELWYLQAET RGLAGNIIGL
HQARAEYFAR VGDYDQALEQ LDFARRRASG NFQLAARIDA RHSELLDEKR AIDQLLR
//
