ID A0A2G0PVY4_9GAMM Unreviewed; 239 AA.
AC A0A2G0PVY4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Peptidase P60 {ECO:0000313|EMBL:PHM51115.1};
GN ORFNames=Xhom_04969 {ECO:0000313|EMBL:PHM51115.1};
OS Xenorhabdus hominickii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM51115.1, ECO:0000313|Proteomes:UP000225433};
RN [1] {ECO:0000313|EMBL:PHM51115.1, ECO:0000313|Proteomes:UP000225433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM51115.1,
RC ECO:0000313|Proteomes:UP000225433};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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:PHM51115.1}.
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DR EMBL; NJAI01000031; PHM51115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G0PVY4; -.
DR STRING; 351679.A9255_18770; -.
DR Proteomes; UP000225433; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08073; MPN_NLPC_P60; 1.
DR Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR InterPro; IPR028090; JAB_dom_prok.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR34858; CYSO-CYSTEINE PEPTIDASE; 1.
DR PANTHER; PTHR34858:SF1; CYSO-CYSTEINE PEPTIDASE; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR Pfam; PF14464; Prok-JAB; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF102712; JAB1/MPN domain; 1.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 2..128
FT /note="MPN"
FT /evidence="ECO:0000259|PROSITE:PS50249"
FT DOMAIN 99..235
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
SQ SEQUENCE 239 AA; 27260 MW; 5AFCE159615826BB CRC64;
MDILRKSMVN AIMTHAEAEY PNECCGLVIQ NSRRQEYIRC RNTAPSPTEQ FCLHPEDYAE
AEDAGTIVAI VHSHPDATTQ PSQLDIAQCD LSQVPWVIAS WPEGDIRTVM PTEGVKPLLG
RPFVHGIWDC YAIVRDWYRL ERNIEIPNFA RSEGWWNRGE NLYMKHYAGA GFTECSGGLQ
VGDVIIMQVQ ANEPNHAGVY IGDGLMLHHL YGQLSNRVPY DGYWQDRTIK TLRYNKLHK
//
