ID A0A1Y3P118_9PSED Unreviewed; 460 AA.
AC A0A1Y3P118;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:OUM72191.1};
GN ORFNames=AUC60_19920 {ECO:0000313|EMBL:OUM72191.1};
OS Pseudomonas caspiana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1451454 {ECO:0000313|EMBL:OUM72191.1, ECO:0000313|Proteomes:UP000195440};
RN [1] {ECO:0000313|EMBL:OUM72191.1, ECO:0000313|Proteomes:UP000195440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBF102 {ECO:0000313|EMBL:OUM72191.1,
RC ECO:0000313|Proteomes:UP000195440};
RX PubMed=28552245; DOI=10.1016/j.syapm.2017.04.002;
RA Busquets A., Gomila M., Beiki F., Mulet M., Rahimian H., Garcia-Valdes E.,
RA Lalucat J.;
RT "Pseudomonas caspiana sp. nov., a citrus pathogen in the Pseudomonas
RT syringae phylogenetic group.";
RL Syst. Appl. Microbiol. 40:266-273(2017).
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:OUM72191.1}.
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DR EMBL; LOHF01000019; OUM72191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3P118; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000195440; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..460
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013050976"
FT TRANSMEM 433..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..148
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 190..362
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 460 AA; 52052 MW; 4A49C8BDD8DADA40 CRC64;
MRCLLFACLF LIALPSSALD RFQVEGYLLP NGLQLLLKPG YEKGHVAIRL VVGIGFDDFP
CEDKELPHLL EHLLFSGIDD AGEGGLEERM QVLGGDWNAF TSNTDTTFVI EAPAQNQRKV
LDLLLDVLTK THFDQADLDT VKRIVEREDG GHYSHLQRWL DRKDLGHSAS SQLAVEMGLK
CAERPQVDHI TLEQVQEVFS SWYAPNNMTL VMVGDLDRLL PGYLERTFGE LDALDPIEHP
PLAEANDKAE KDRTLIRGAL GDAARLHLIF KEPLLDDQHD ETLELVSDYL EWALYSDLRL
KHGLSYGPWV DREVFGGSGF MSLNADLERD DVDQAKEYVR AMLERLQTDG LDPAAFARVK
QATIAKQAWA VQGNSALADY YWGALNDYEN GRFADPGKRY KAVSLDNANR ALRELLKQKS
YWRTEQSLLS YDGLFWLTTA VLGFVVLLVG WRVSAYRRHR
//
