ID   A0A1H8TE37_9ACTN        Unreviewed;       433 AA.
AC   A0A1H8TE37;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Membrane-associated protease RseP, regulator of RpoE activity {ECO:0000313|EMBL:SEO89182.1};
GN   ORFNames=SAMN05660991_02173 {ECO:0000313|EMBL:SEO89182.1};
OS   Trujillella endophytica.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Trujillonella.
OX   NCBI_TaxID=673521 {ECO:0000313|EMBL:SEO89182.1, ECO:0000313|Proteomes:UP000198960};
RN   [1] {ECO:0000313|EMBL:SEO89182.1, ECO:0000313|Proteomes:UP000198960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45413 {ECO:0000313|EMBL:SEO89182.1,
RC   ECO:0000313|Proteomes:UP000198960};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOEE01000006; SEO89182.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8TE37; -.
DR   STRING; 673521.SAMN05660991_02173; -.
DR   Proteomes; UP000198960; 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; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 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, ECO:0000313|EMBL:SEO89182.1};
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        106..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..364
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        406..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          137..235
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   433 AA;  46247 MW;  165C67CBE2E1CEDF CRC64;
     MWARKFGMRV PQFFVGFGPT VFSRTRGETE FGIKAIPMGG YIRIVGMIPP AEEGESKRAT
     RMRSFIAEVR GQALNDVRPG DEGRVFYAKP WWQRVIVMSA GPLHNLLLAV VFFAITLTAV
     GTSVITTQVR SVPACVVPAG AQSIDRAAAD DSDVCDIPIV TSGAEAGEVC DLGTPNCALP
     VASPAARAGL QPGDTIVAVG GESVDPTAYD SWTTVQQAIR NSPGEELALT IERDGERQEL
     TVTPIENTVL TDDGDGTMTA GYLGVSPVGG FARQGIGEMP GYFGMIVTNS IERLVEIPER
     VPQLFRAAFL GEERDEQGPI GVVGVGRISG EVFSIEDFSN GEKLSFFLSL LASVNLVLFL
     FNLLPMYPLD GGHVAGALYE KGRSTVARWR GRPDPGPFDI ARLMPVAYVV AGLFIALSGL
     LLVADVVNPI TLQ
//