ID A0A3A1U500_9MICO Unreviewed; 470 AA.
AC A0A3A1U500;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:RIX31433.1};
GN ORFNames=D1781_07150 {ECO:0000313|EMBL:RIX31433.1};
OS Amnibacterium setariae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Amnibacterium.
OX NCBI_TaxID=2306585 {ECO:0000313|EMBL:RIX31433.1, ECO:0000313|Proteomes:UP000265742};
RN [1] {ECO:0000313|Proteomes:UP000265742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD4a {ECO:0000313|Proteomes:UP000265742};
RA Kim I.;
RL Submitted (SEP-2018) 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:RIX31433.1}.
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DR EMBL; QXTG01000001; RIX31433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A1U500; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000265742; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000265742};
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 155..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 393..419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 440..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..423
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 213..257
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 470 AA; 49248 MW; 4E9C09C2739872CA CRC64;
MEPLLYLAGV LVILVGVVVS IGLHEVGHLL PAKLFGVRVT QYMIGFGRTV WSRRRGETEY
GFKAIPLGGY ISMVGMFPPA KQGRRERLFQ GRPPATAGEA VEDVVEEVEA PSRGRTASTG
FFNTLVQDAR DSSQDQIQPG EEHRAFYRLA VWKRVVIMLG GPTVNLILGI LFTGILLTGF
GVVTPTTTVA AISQCIVPAT QTRDTCTASD APAPAAGTAL KPGDRITAID GKPVSTWDDV
TAVIRTSAGR PIELTVAAKA GGTERITVTP ATNTVPVTNA AGAVEKDANG ATRTQTVGFI
GITSTEALQR QPVTAVVPAV WNNVTAVAGV IVNLPARLVG VAQAAFGSGE RDPNGPISVV
GVGRVAGEIA ANPQVTVTSK VASLVGILGS LNIALFVFNL IPLLPLDGGH VIGALWEGLR
RRVARLLGRR DPGPVDTAKL MPLTFAVAIL LGGMSVLLIY ADLVRPISIF
//
