ID A0A0Q0HZN1_PSESX Unreviewed; 471 AA.
AC A0A0Q0HZN1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase, M16 family protein {ECO:0000313|EMBL:KPY94255.1};
GN ORFNames=ALO94_05386 {ECO:0000313|EMBL:KPY94255.1};
OS Pseudomonas syringae pv. spinaceae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=264459 {ECO:0000313|EMBL:KPY94255.1, ECO:0000313|Proteomes:UP000050384};
RN [1] {ECO:0000313|EMBL:KPY94255.1, ECO:0000313|Proteomes:UP000050384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP16929 {ECO:0000313|EMBL:KPY94255.1,
RC ECO:0000313|Proteomes:UP000050384};
RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT "Genome announcement of multiple Pseudomonas syringae strains.";
RL Submitted (SEP-2015) 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:KPY94255.1}.
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DR EMBL; LJRI01000647; KPY94255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0HZN1; -.
DR PATRIC; fig|264459.3.peg.5986; -.
DR Proteomes; UP000050384; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..160
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 202..373
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 246..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 52961 MW; 8AF52D97E060FE31 CRC64;
MLNIPARQES CFMRCLLFAC LLLGSLPSFA LDRLQVEGYL LPNGLQVLLK PGYEKGHVAI
RLVVGIGFDD FPCQDKELPH LLEHLLFSGI DDGGEGGLEE RMQALGGEWN AFTSNADTTF
VIEAPARNQR KVLDLLLEIM TRTELSQARL DGVKRVVERE DGGHFSHLQR LLDRRDSGRS
AISQLAVEMG LKCAERPEVD GIKLEHIEDV FANWYAPNNM TLIVVGDLDK LLPAYLERTY
GKLAPTDPID HPPLAPGSGS AQARQELQRG GLGESAKLHL IYPEPQLDDQ HDETWDLVKA
YLDWALYTEL RLKRSLSYGP SAEREVFGDV GFLSLNADVE RNDTDEAERD IRALVERLQK
DGMQPATFAR LQQLAIDRQS WATQGNSALA DYYWSALNDY EKGRFEDPAK RIKAVKLETA
NQAMRQLLAQ PGYMRIEEPL FSYDGLYWLA GGVLGLIVLL AVWRWRARGK T
//
