ID A0A229UJU0_9BACL Unreviewed; 479 AA.
AC A0A229UJU0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Peptidase A2 {ECO:0000313|EMBL:OXM83662.1};
GN ORFNames=CF651_24555 {ECO:0000313|EMBL:OXM83662.1};
OS Paenibacillus rigui.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=554312 {ECO:0000313|EMBL:OXM83662.1, ECO:0000313|Proteomes:UP000215509};
RN [1] {ECO:0000313|EMBL:OXM83662.1, ECO:0000313|Proteomes:UP000215509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16352 {ECO:0000313|EMBL:OXM83662.1,
RC ECO:0000313|Proteomes:UP000215509};
RA Mayilraj S.;
RT "Genome sequencing and assembly of Paenibacillus rigui.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:OXM83662.1}.
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; NMQW01000040; OXM83662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A229UJU0; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000215509; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000215509};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 369..460
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 20..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 50602 MW; 93C741F822D823F2 CRC64;
MDNNRNDEQY NYFYKGASTS EVYRHEPDNE NRTKEPIDVT PQRPGRFFGY SGEVSLNSGG
KGPGKKRSAL ISTFAAFMAG ALVVSSLMFA ADKYNLFTGN SAAAAPTQQS STAGSSNGSG
AKTASLNTIT NGSVADIAKQ AGPAVVKIET KVKAANAGSS SMFNDPLFRQ FFGNNGGGQG
QQGGSGQDSN SLQPGGIGSG FIFQSSGYIL TNEHVVDGAA EIEVTVQGYD QPFKATLLGN
SYDLDLAVLK IEGDKEFPTL PIGNSDNTQV GDWVVAIGNP YDFDYTVTSG VISAKERPIS
IPDDKGTRNY KHLLQTDAAI NPGNSGGPLL NMNGEVIGIN TAVNSEAQGI GFAIPTSTIS
SVLENLKNNV TIPKEPSPYI GVSLQNLTND MLSELNLKNT DGALVADIQP KTPGFEAGLR
QYDVIVAADG TKITSTTELT KKVQAAKVGD KMQLTIIRNG EQKEITVTIG DRNANLQKK
//
