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Database: UniProt
Entry: W1IUV2_9GAMM
LinkDB: W1IUV2_9GAMM
Original site: W1IUV2_9GAMM 
ID   W1IUV2_9GAMM            Unreviewed;       257 AA.
AC   W1IUV2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Putative tail assembly protein {ECO:0000313|EMBL:CDL80970.1};
GN   Name=K {ECO:0000313|EMBL:CDL80970.1};
GN   ORFNames=XSR1_100021 {ECO:0000313|EMBL:CDL80970.1};
OS   Xenorhabdus szentirmaii DSM 16338.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL80970.1, ECO:0000313|Proteomes:UP000019202};
RN   [1] {ECO:0000313|EMBL:CDL80970.1, ECO:0000313|Proteomes:UP000019202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL80970.1,
RC   ECO:0000313|Proteomes:UP000019202};
RA   Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT   "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT   Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT   16338.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:CDL80970.1}.
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DR   EMBL; CBXF010000002; CDL80970.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1IUV2; -.
DR   STRING; 1427518.XSR1_100021; -.
DR   Proteomes; UP000019202; 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; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000019202};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          6..134
FT                   /note="JAB1/MPN/MOV34 metalloenzyme"
FT                   /evidence="ECO:0000259|SMART:SM00232"
SQ   SEQUENCE   257 AA;  29302 MW;  44523330104268F6 CRC64;
     MIQEMMNTAL YLAMQQAAIQ TYPNEACGLL VNTKRAKYEL VLCKNVAEDP VNFFVMDAED
     QIAAENKGEV VGVWHSHTDR TNKASEADLA GCESSEIPWF IINVTKNYNP EIDSEFIISD
     VNVITPNGFE MPYEGRPYAF GVFDCWMLCR DYLKREFNIQ VGACSHLHIP NWWDGDKDIL
     SENFAEQGFV KLPYGTQPKR GDLFLMKIGA KMPDHCAVYI GDNLILHHQS DRLSCKAVYG
     GMYQKTTIHH LRHKELL
//
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