ID A0A0Q4RPQ0_9BACL Unreviewed; 222 AA.
AC A0A0Q4RPQ0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:KQO17667.1};
GN ORFNames=ASF12_03080 {ECO:0000313|EMBL:KQO17667.1};
OS Paenibacillus sp. Leaf72.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO17667.1, ECO:0000313|Proteomes:UP000051722};
RN [1] {ECO:0000313|EMBL:KQO17667.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO17667.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO17667.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO17667.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:KQO17667.1}.
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DR EMBL; LMLV01000001; KQO17667.1; -; Genomic_DNA.
DR RefSeq; WP_056029366.1; NZ_LMLV01000001.1.
DR AlphaFoldDB; A0A0Q4RPQ0; -.
DR STRING; 1736234.ASF12_03080; -.
DR OrthoDB; 9800627at2; -.
DR Proteomes; UP000051722; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06158; S2P-M50_like_1; 1.
DR InterPro; IPR008915; Peptidase_M50.
DR InterPro; IPR044537; S2P-M50-like.
DR PANTHER; PTHR35864; ZINC METALLOPROTEASE MJ0611-RELATED; 1.
DR PANTHER; PTHR35864:SF1; ZINC METALLOPROTEASE YWHC-RELATED; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:KQO17667.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KQO17667.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051722};
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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..186
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 222 AA; 24844 MW; D9FFDAECE0CD0994 CRC64;
MEGWFAYPTA ELPFAVLVLI IAFTVHEFAH AYTAYKFGDN TAYDAGRVTL NPRVHLDVLG
MILILLAGFG WAKPVPVNQN RFKHPRLMGV IVTAAGPLSN FVLGLLGIIL YYLSIKTGLY
HMGSIGVQDA LQVFFSYFIS LNFLLFIFNL IPLPPLDGYR IIQNLVPLKV GYKMEQNMQW
GIIIFLLLLF IPPLRAVTIS PILNFSQELA AYFMGLLGGL FI
//