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}.
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; 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
//