ID A0A1E8CW98_9MICO Unreviewed; 448 AA.
AC A0A1E8CW98;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:OFE16625.1};
GN ORFNames=BA895_03290 {ECO:0000313|EMBL:OFE16625.1};
OS Humibacillus sp. DSM 29435.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Humibacillus.
OX NCBI_TaxID=1869167 {ECO:0000313|EMBL:OFE16625.1, ECO:0000313|Proteomes:UP000175826};
RN [1] {ECO:0000313|Proteomes:UP000175826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29435 {ECO:0000313|Proteomes:UP000175826};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-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:OFE16625.1}.
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DR EMBL; MAST01000012; OFE16625.1; -; Genomic_DNA.
DR RefSeq; WP_070191763.1; NZ_MAST01000012.1.
DR AlphaFoldDB; A0A1E8CW98; -.
DR STRING; 1869167.BA895_03290; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000175826; 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 ECO:0000313|EMBL:OFE16625.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OFE16625.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000175826};
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 126..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 420..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..400
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 192..233
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 448 AA; 47549 MW; 94D9282E881D0000 CRC64;
MLFILGVLVI VVGVALSIAL HEIGHLLPAK KFGVKVTQYM VGFGPTVWSR KRGETEYGIK
AIPLGGYVRM IGMLPPRPGD KPGELRTLST GRFSQMVDQA RADALEEVAP GDEDRVFYKL
HPAKKIIIML GGPMVNLVIA AVLLTGVITL YGLPQVVPKV GLLSACVPTA APTLALPQPT
CAPGDPQAPS VAGGLQQNDR ILSVDSAPIT TWDQVTAAIR DHAGQSLQMV VQRGDQQVPI
TVTPASLERA TYDAEGNPVT KDGQLVLAKT GFLGVTPGQD LVKTPIWDAP QFVWKQAVQT
ASIIVKIPQK MAGVVQAAFG SGERDPNGPI SVVGVGRIGG EVAAADIPAD EGGNWLKLIQ
LVLLVASLNL ALFVFNLVPL LPLDGGHVAG AIWEWVKRTV ARLRDRPDPG YVDVAKGLPI
AYGMSLVLIT MSVLLIYADI VKPIRLFG
//
