ID A0A2Y9AF40_9MICO Unreviewed; 437 AA.
AC A0A2Y9AF40;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Membrane-associated protease RseP, regulator of RpoE activity {ECO:0000313|EMBL:SSA41898.1};
GN ORFNames=SAMN05216184_105142 {ECO:0000313|EMBL:SSA41898.1};
OS Georgenia satyanarayanai.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=860221 {ECO:0000313|EMBL:SSA41898.1, ECO:0000313|Proteomes:UP000250222};
RN [1] {ECO:0000313|EMBL:SSA41898.1, ECO:0000313|Proteomes:UP000250222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10826 {ECO:0000313|EMBL:SSA41898.1,
RC ECO:0000313|Proteomes:UP000250222};
RA Cai Z.;
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; UETB01000005; SSA41898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9AF40; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000250222; 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; 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 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:SSA41898.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000250222};
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 123..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..389
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 177..225
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 437 AA; 46024 MW; 734D8221670B7E19 CRC64;
MSFLVGVLVL VVGLVISIAL HEVGHLVPAK RFGVKVTEYF VGFGPTLWSR RRGETEYGVK
AVPLGGYVRM VGMYPPARSD RPVRRRRDGR ATLVEEAREY ALAEVGPGEE HRTFSSLSVP
KKLVVMLGGP VMNLLIAVVL LSVVLVGVGV PAYTATLGNV QECLPADQAA TECSDTDPAA
PGEVAGLQPG DTVVSWGGRP VEGWDDVRAA IAASGPSPAT VVVERDGQER TVTVTPAMSE
RPVVVDGEVL TDDAGEPVTE PQPFVGIGPV AELVPQPVSA VPGRVVEAVG ATFEVVLTLP
QRLVDVAQAA FGEEERDPGV VGLVGVGRFA GEIASIDSER YGVVERAADL LGLLASLNLA
LFVFNLIPLL PLDGGHIAGA LWEGLRRRVA AWRGRPDPGP VDVARMLPLT YVVVVAMVGM
SLLLAYADIV RPVTLTG
//
