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Database: UniProt
Entry: A0A433SDU0_9BURK
LinkDB: A0A433SDU0_9BURK
Original site: A0A433SDU0_9BURK 
ID   A0A433SDU0_9BURK        Unreviewed;       486 AA.
AC   A0A433SDU0;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   SubName: Full=Putative zinc protease {ECO:0000313|EMBL:RUS66856.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:RUS66856.1};
DE   Flags: Precursor;
GN   ORFNames=CUZ56_01651 {ECO:0000313|EMBL:RUS66856.1};
OS   Saezia sanguinis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Saezia.
OX   NCBI_TaxID=1965230 {ECO:0000313|EMBL:RUS66856.1, ECO:0000313|Proteomes:UP000286947};
RN   [1] {ECO:0000313|EMBL:RUS66856.1, ECO:0000313|Proteomes:UP000286947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNM695-12 {ECO:0000313|EMBL:RUS66856.1,
RC   ECO:0000313|Proteomes:UP000286947};
RA   Medina-Pascual M.J., Valdezate S., Monzon S., Cuesta I., Carrasco G.,
RA   Villalon P., Saez-Nieto J.A.;
RT   "Saezia sanguinis gen. nov., sp. nov., in the order Burkholderiales
RT   isolated from human blood.";
RL   Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:RUS66856.1}.
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DR   EMBL; PQSP01000003; RUS66856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433SDU0; -.
DR   Proteomes; UP000286947; Unassembled WGS sequence.
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:UniProtKB-KW.
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; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF49; MITOCHONDRIAL-PROCESSING PEPTIDASE SUBUNIT ALPHA; 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:0000313|EMBL:RUS66856.1};
KW   Protease {ECO:0000313|EMBL:RUS66856.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286947};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..486
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019551240"
FT   DOMAIN          61..201
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          210..400
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   486 AA;  53868 MW;  B307D8E7749C94FE CRC64;
     MVRFTYILTW VLCMVVTPAW AQPASEASVV PAPAQQSSAA TEPQVYEYRL DNGMTLWVKP
     DHRAPTVTHM VWYRVGSRDE VDGTSGVAHM LEHMMFRGTS AIPGGGFSRR VAELGGDDNA
     FTSYDMTAYY QQIPNQALPE VMRMEADRMR NLTLNEADFL KELEVVKEER RMRTDERPRA
     QLWEQLRATT FMADPYHRPV IGWMSDLDAM TVNDAREFYQ RWYRPDNAAV IIVGDVQPED
     ALQMATQTYG KIATPATALA PGKPRTEPQQ QGIRRIEHKA PAAQSYVALA FKVPGIASWD
     KDDAQSQDAY ALTLLAAVLD GTSSSRLQRQ LVQGEGGKRI ADSASAGYEL VARGPVLFVV
     SGVPAQGHTP EELEQALRAE IARIAREGVD AKELQRIKTQ WVASQVYQND SLMSQAQDLG
     SNWILYAPPL ATDLLLERLR EVTPEQVQAV AARYFGDDQL TVGILRAQPL PAGAAAQDED
     APAALH
//
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