ID   A0A1Y3G327_9PROT        Unreviewed;       425 AA.
AC   A0A1Y3G327;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Peptidase M29 {ECO:0000313|EMBL:OUI87567.1};
GN   ORFNames=HK11_10915 {ECO:0000313|EMBL:OUI87567.1};
OS   Acetobacter sp. DmW_043.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=1670658 {ECO:0000313|EMBL:OUI87567.1, ECO:0000313|Proteomes:UP000196359};
RN   [1] {ECO:0000313|EMBL:OUI87567.1, ECO:0000313|Proteomes:UP000196359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DmW_043 {ECO:0000313|EMBL:OUI87567.1,
RC   ECO:0000313|Proteomes:UP000196359};
RA   Ju J., Zhang J.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M29 family.
CC       {ECO:0000256|ARBA:ARBA00008236}.
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:OUI87567.1}.
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; JOMN01000041; OUI87567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y3G327; -.
DR   Proteomes; UP000196359; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
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   Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR34448:SF3; AMINOPEPTIDASE AMPS; 1.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
DR   SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196359}.
SQ   SEQUENCE   425 AA;  46063 MW;  DF72E11BF003630A CRC64;
     MSDKKNFLQD GRAGDNRFAA MLDRLGEVAV RTGLNIKPGQ QLIITAPLES APLVRRITEH
     AYKAGSSLVT TFYSDDEATL ARYRYGHDET FDTAAGWLAH GMTEGFREGA ARLAITGSDP
     VLLADQDPSR ISRAARAASV VNRPAMKIIT SFDVNWTIVA ASTVAWARQV FPFLQDDEAV
     SELWQAIFKA SRITGEDPVA EWAAHNTQLH KRAAFLNDAR YEALHFTGPG TDLTVGLADG
     HHWAGGAEKA GNGVICNPNL PTEEVFTTPH RLKVEGHVVS SKPLFHQGSL IDGISVRFEG
     GKITEMHAVK GQDVLARILD TDEGARRLGE VALVPHSSPI SQSGILFKNT LFDENAASHI
     ALGQAYSKCM RDAEGLDDTA LAARGANNSI LHIDWMIGSG ETDVDGLTSD GQRVKLMRKG
     EWVIS
//