ID   A0A061QGG1_9PROT        Unreviewed;       913 AA.
AC   A0A061QGG1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative zinc protease y4wA {ECO:0000313|EMBL:GAK33329.1};
GN   ORFNames=AQ1_01217 {ECO:0000313|EMBL:GAK33329.1};
OS   alpha proteobacterium Q-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK33329.1, ECO:0000313|Proteomes:UP000027360};
RN   [1] {ECO:0000313|EMBL:GAK33329.1, ECO:0000313|Proteomes:UP000027360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q-1 {ECO:0000313|EMBL:GAK33329.1,
RC   ECO:0000313|Proteomes:UP000027360};
RX   PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA   Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA   Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT   "Iodide oxidation by a novel multicopper oxidase from the
RT   alphaproteobacterium strain Q-1.";
RL   Appl. Environ. Microbiol. 78:3941-3949(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:GAK33329.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BAYV01000013; GAK33329.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061QGG1; -.
DR   STRING; 1492281.AQ1_01217; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000027360; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:GAK33329.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027360};
KW   Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..913
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001608978"
FT   DOMAIN          44..177
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          202..377
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          488..623
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          643..822
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   913 AA;  99300 MW;  6E7B4D23418669F7 CRC64;
     MTFPGFLKRA LIAASFCFGG AALAVEMPAV DIPYESFTLE NGLRVVVHED RKAPVVAVSV
     WYHVGSKNEP VGKTGFAHLF EHLMFNGSEN YDGEFFEPLQ EVGVTDINGT TWLDRTNYFE
     TVPTPALERA LFLESDRMGH LLGAVTQEKL DNQRGVVQNE KRQGENQPYG RAFEALQKGV
     FPVGHPYHHS TIGSMADLDA ASLDDVKEWF KTYYGPNNSV LVLAGDINVA QARDLVTRYF
     GDIPAGPPLS QAKAAIPELN SNVREVMEDR VPQARVYRVW AVPGRTTQSA AVLDVAAEIL
     GGGKTSRLYR DLAYDRQIAT NIQVGLFPFE LSSLFFIQAD VKDGESVAEV SSRIDQVVAD
     FLAKGPTKAE LERAQIGLIG EDVRALEKVG GFGGKAVTLA EGALYAGDPG FYKTRLQRIA
     GASINDVKTQ SAQWLSRHHY QLEVTPFGEF TAAAGGIDRT GGLPGVDESP ELDFPAIETA
     TLSNGIEVVL ANRATVPIVN ISVMFDAGFA ADRGLKLGSA SLTLEMLDEG TKKRSALKIA
     EELESLGAQL NTGSNLDVST VALNALKTEL AGSVDILADV VRNPAFSATE LERLRQQRLA
     RIRQEESQPV SIALRQLPPI LYGDDHAYGI PFTGSGTLQS VASISRDDLI AYHQSWLRPD
     NARIFVVGDS TMADIKPILE KAFGDWKATG AKAPEKAIDQ VDLPKTGKII IVDRPGSPQS
     LILAGHLAPA TGAENNIAIT TMNDILGGQF TARVNMNLRE EKGWAYGAYT FMQDARGQRP
     FFVYAPVQTD KTALSMAELV VELKAITGDK PATEDELVMA VRNNVRSLPG QFETARDVLG
     AMLANARFGR ALDYEESLKQ RYEQLDLAAI EQAANQVLHP DQLVWMVIGD RAKIEDEIRA
     LDLGEVIVQG GQN
//