ID A0A419V5Q8_9BACL Unreviewed; 429 AA.
AC A0A419V5Q8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 10.
DE SubName: Full=Putative Zn-dependent peptidase {ECO:0000313|EMBL:RKD75322.1};
GN ORFNames=ATL39_1021 {ECO:0000313|EMBL:RKD75322.1};
OS Sinobaca qinghaiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae; Sinobaca.
OX NCBI_TaxID=342944 {ECO:0000313|EMBL:RKD75322.1, ECO:0000313|Proteomes:UP000285120};
RN [1] {ECO:0000313|EMBL:RKD75322.1, ECO:0000313|Proteomes:UP000285120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17008 {ECO:0000313|EMBL:RKD75322.1,
RC ECO:0000313|Proteomes:UP000285120};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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:RKD75322.1}.
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; RAPK01000007; RKD75322.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419V5Q8; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000285120; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
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:UP000285120};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 63..175
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 181..361
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 429 AA; 48704 MW; 1767A45B537015AF CRC64;
MNTLEKSTID EKLYYEVLDN GLQVYILPKK GFHKTFATFT TNYGSIDNHF TPIGGSEPVK
VPDGIAHFLE HKMFEDEEGD VFQTFGKQGA SSNAFTSFTK TAYLFSSTAQ TEKNISTLLD
FVQHPYFTED SVEKEKGIIE QEIRMYEDQA DWLAFFQLLG GMYHEHPAKI DIAGTVESIY
DITKEDLYTC YETFYHPSNM ALFIAGDAEP EALMALIKEN QAGKEFPPAP ELKRILPEEP
AEAASDKKVL EMSVNTPKVL VGYKVLQERT GEDLMRYELA MDLLMDTLIG PGTTFYESLY
EEGLIDDSFS GEFQVDRSFT FFVAGGDTAQ PDELQNRITS LLETKDPAAF DSEMFERIKR
RNIGTFLRQL NSLEFMASQY TSYAFAGMDM FDTAAMLESI TAEECLELWN QHFHGPERSV
SQVVKKKNE
//
