Y1964_AQUAE
ID Y1964_AQUAE Reviewed; 429 AA.
AC O67776;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative zinc metalloprotease aq_1964;
DE EC=3.4.24.-;
GN OrderedLocusNames=aq_1964;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07743.1; -; Genomic_DNA.
DR PIR; D70468; D70468.
DR RefSeq; NP_214345.1; NC_000918.1.
DR RefSeq; WP_010881281.1; NC_000918.1.
DR PDB; 3WKL; X-ray; 2.80 A; A=113-292.
DR PDB; 3WKM; X-ray; 2.20 A; A/B=115-292.
DR PDB; 6AKQ; X-ray; 1.90 A; A=115-292.
DR PDB; 6AL0; X-ray; 2.60 A; A=115-292.
DR PDB; 6AL1; X-ray; 3.20 A; A=115-292.
DR PDB; 6ICC; X-ray; 2.00 A; A=115-292.
DR PDB; 6ICF; X-ray; 4.00 A; A=115-292.
DR PDB; 7CQD; X-ray; 3.20 A; A/B=115-292.
DR PDBsum; 3WKL; -.
DR PDBsum; 3WKM; -.
DR PDBsum; 6AKQ; -.
DR PDBsum; 6AL0; -.
DR PDBsum; 6AL1; -.
DR PDBsum; 6ICC; -.
DR PDBsum; 6ICF; -.
DR PDBsum; 7CQD; -.
DR AlphaFoldDB; O67776; -.
DR SMR; O67776; -.
DR STRING; 224324.aq_1964; -.
DR ABCD; O67776; 1 sequenced antibody.
DR EnsemblBacteria; AAC07743; AAC07743; aq_1964.
DR KEGG; aae:aq_1964; -.
DR PATRIC; fig|224324.8.peg.1515; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_2_0; -.
DR InParanoid; O67776; -.
DR OMA; QYMVGFG; -.
DR OrthoDB; 1395197at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
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; PTHR42837; 2.
DR Pfam; PF17820; PDZ_6; 2.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR TIGRFAMs; TIGR00054; TIGR00054; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..429
FT /note="Putative zinc metalloprotease aq_1964"
FT /id="PRO_0000088427"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 189..265
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT ACT_SITE 18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6AKQ"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6AKQ"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:6AKQ"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:6AL0"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:6AKQ"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6AKQ"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:6AKQ"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:3WKM"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:6AKQ"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:6AKQ"
SQ SEQUENCE 429 AA; 47792 MW; 4EB336169F7D613B CRC64;
MGLIAFLILI GVLVWVHEFG HFLMAKLFRV KVEIFSIGFG PPIFRRQWGE TVYQIAALPL
GGYVKLYGEE ENVHDPRAFS TKKPWQKILI ALGGPLFNFL FTILVFALVY TAGVEVPKYL
KEPVVVGYVQ RDSIAQKIGI KPGDKIIKIN GYEVRTWEDL RDALIRLSLD GVKETTLFLE
RNGEVLHLTI KVPNVQKGEE LGIAPLVKPV VGGVKKGSPA DQVGIKPGDL ILEVNGKKIN
TWYELVEEVR KSQGKAIKLK ILRNGKMIEK ELIPAKDPKT GTYFIGLFPK TETVVEKKPF
GEALASAVNR TWELTVLTLK TIAGLITGKV SFQTLGGPIA IAQIAGQAAQ SGFIPYLVMM
AFISLQLGIF NLIPLPILDG GLILLFAIEW LRGRPLPEKF KEYWQRVGLA IIITLTIFVF
INDILRLLR
