ID A0A4V3D6M9_9GAMM Unreviewed; 913 AA.
AC A0A4V3D6M9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:TDQ44567.1};
GN ORFNames=EV696_12449 {ECO:0000313|EMBL:TDQ44567.1};
OS Permianibacter aggregans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Permianibacter.
OX NCBI_TaxID=1510150 {ECO:0000313|EMBL:TDQ44567.1, ECO:0000313|Proteomes:UP000295375};
RN [1] {ECO:0000313|EMBL:TDQ44567.1, ECO:0000313|Proteomes:UP000295375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103792 {ECO:0000313|EMBL:TDQ44567.1,
RC ECO:0000313|Proteomes:UP000295375};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TDQ44567.1}.
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DR EMBL; SNYM01000024; TDQ44567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3D6M9; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000295375; 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; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 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:TDQ44567.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295375};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..913
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5020394305"
FT DOMAIN 41..165
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 200..372
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 484..612
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 640..816
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 913 AA; 100908 MW; 6C484DB50884F917 CRC64;
MRLSTLSVAT LMVFGSAIVA AADTTTLDIP YTKFTLDNGL RVIVHEDKKA PIVAVNVWYH
VGSKDEKAGR TGFAHLFEHL MFNGSENYND EYFGPFEKVG ATDMNGTTWL DRTNYFQNVP
KTALDMTLWM ESDRMGHMLG AVTQEKLDEQ RGVVQNEKRQ GENQPYGRSF EWLQKGSFPE
GHPYSWTTIG SMEDLNAAKL EDVHEWFKTY YGAANAVVVL AGDIDVETAK SKMNQYFGDI
PAGPPLVKRG AWIAKRDDSK RDIMFDRVPQ VRITKSWNVP TFGSKEADQL ELVAAILGGG
KNSRLYKTLV YDKQMATNVR ADVMQFELAS LFGINVDVKP GVNPAEVEAI INRELALLID
KGPSKKELER VKVTEEANFV RGAERIGGFG GKSDILATYE VYTGEAGNFK RSLEHKLSAS
TKDLQQLAKA WLSSGDYHLE VHPFPNYNTV ASNVDRSKLP EVNSTPDLDF PKVERAMLSN
GLKVLFAERH SVPAVNISLQ IDSGFAADQG SKLGTANFAL SMVDEGTKKL SASEISEKAE
MLGANLGSGC ALDVCSISID MLKAKLDDSL NLFADVVLNP AFDQEEIDRL RGRWLANIAR
EKAQPVSMAF RTLPPLLYGN GHSYAMPFTG SGTEQSITAL NRDDLVAFYQ KWVRPDNATL
VVVGDTTLSE LLPKLEKSLG GWKAPATPKP IKNLANVPMQ DKTQIFLIDK PGAVQSVIIA
GQLMPGFKDD EAALLYAMND IIGGQFTARL NMNLREQKSW AYGAYTIKQN AVGQSPYFAY
APVQIDKTVE SMQEVLNELK AYIGSKPATE AELQKTVLNT VRSQPGEYET MDAVQGALVS
IANYQRPDNY VEQIKARYEA LTVADINAAA KQYLRPQAMT WVVVTDLSKT EQKIRDLKLG
EVTVIDADGN KLR
//