ID Q5P733_AROAE Unreviewed; 457 AA.
AC Q5P733;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE SubName: Full=Predicted Zn-dependent peptidase {ECO:0000313|EMBL:CAI06878.1};
GN ORFNames=ebA1394 {ECO:0000313|EMBL:CAI06878.1};
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06878.1, ECO:0000313|Proteomes:UP000006552};
RN [1] {ECO:0000313|EMBL:CAI06878.1, ECO:0000313|Proteomes:UP000006552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI06878.1,
RC ECO:0000313|Proteomes:UP000006552};
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CR555306; CAI06878.1; -; Genomic_DNA.
DR RefSeq; WP_011236606.1; NC_006513.1.
DR AlphaFoldDB; Q5P733; -.
DR STRING; 76114.ebA1394; -.
DR MEROPS; M16.019; -.
DR KEGG; eba:ebA1394; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_4; -.
DR Proteomes; UP000006552; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006552};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..457
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004261262"
FT DOMAIN 38..183
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 191..373
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 438..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 457 AA; 50429 MW; E4DDF66730D0795E CRC64;
MFRQNFPRIA LLAAALFATA GPLHANPFET TLDNGMQVIV KEDRRAPSVV HMVWYDVGAM
DEPAGVSGIA HLLEHMMFKG TEKVGPGEFN KRVAAVGGRD NAFTSRDYTA YFQQIPPAEL
DDMMMLEADR MANLKITPSL FAPELDVVRE ERRLRTEDEP RALVHEQLMA TTFQAHPYGR
PVIGWMTDLA SMTAEDARTW HRNWYAPNNA RLVVVGDVDH QAVFDLARRH YGAVAARDLP
KRRVTPEPEQ LGPRQSVVRA PAELPYVALA WRAPTLRDPA NDRDVYALQV LAAVLDGYDG
ARLPRRLVRE TRVAVSVGAG YDGTARGPSL FTLDAAPAVG KTVADVAAAL RDEIARIQKE
GIAEDELERV KTQTIAGEVY KRDSLMGQAM EIGFLEASGL SWRDEAALLE GVRRVTAAEV
QAVARKYFTD TTLTRAQLDP LPVPAGQPRP AAPATRH
//
