ID A0A1Q5Q5N0_9ACTO Unreviewed; 465 AA.
AC A0A1Q5Q5N0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peptidase M50 domain-containing protein {ECO:0000259|Pfam:PF02163};
GN ORFNames=BSZ39_00080 {ECO:0000313|EMBL:OKL55138.1};
OS Bowdeniella nasicola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Bowdeniella.
OX NCBI_TaxID=208480 {ECO:0000313|EMBL:OKL55138.1, ECO:0000313|Proteomes:UP000185628};
RN [1] {ECO:0000313|Proteomes:UP000185628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19116 {ECO:0000313|Proteomes:UP000185628};
RA Meng X.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family.
CC {ECO:0000256|ARBA:ARBA00007931}.
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:OKL55138.1}.
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; MQVR01000001; OKL55138.1; -; Genomic_DNA.
DR RefSeq; WP_073715364.1; NZ_MQVR01000001.1.
DR AlphaFoldDB; A0A1Q5Q5N0; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000185628; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00989; PDZ_metalloprotease; 1.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000185628};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 162..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..423
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT REGION 80..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 48827 MW; 19DA1F934D386D52 CRC64;
MAYLIGIGLL IIGLLVSIAL HEIGHMAPAK RFGVKVPQYF VGFGPTLWST KRGETEYGIK
AIPLGGYVRL AGMYPPERAI TKDDAGAHSH DVDGPTDAST AATPSHVGSR PDAPADAARR
RPESRSAERR SLASEARAEA LADLAPGEEH RAFYHLSVPK KIVVMLGGPL MNLVIAFVLL
SGIIVGYGLP TLTPTVSAVA ECATDADPCT EPGAAYAAGL RAGDTITSFA GTPITTWQDL
PKAVEKNGLQ PTNITFISDG VEHTARITPQ KREVRIDANT VQERVVISVT AGQERRPGTI
GQAAAMTGTA VTETFKVIGA LPMRLYDVAR SLVTDEPRQD GVMSIIGVGR IAGEVASSPS
DAGGSGGLAG PTWGDRIMSL LSLVASLNIA LFAFNLIPLL PLDGGHIAGA LFEGARRQIA
KLRGAPDPGP VDIARMLPLT YTVFILLIAM TLLLGYADIV KPITL
//
