ID I0QWJ5_9GAMM Unreviewed; 513 AA.
AC I0QWJ5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Peptidase M16 domain-containing protein {ECO:0000313|EMBL:EIC85668.1};
GN ORFNames=SPM24T3_04996 {ECO:0000313|EMBL:EIC85668.1};
OS Serratia sp. M24T3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=932213 {ECO:0000313|EMBL:EIC85668.1, ECO:0000313|Proteomes:UP000011072};
RN [1] {ECO:0000313|EMBL:EIC85668.1, ECO:0000313|Proteomes:UP000011072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M24T3 {ECO:0000313|EMBL:EIC85668.1,
RC ECO:0000313|Proteomes:UP000011072};
RX PubMed=22740681; DOI=10.1128/JB.00670-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Serratia sp. Strain M24T3, Isolated from Pinewood
RT Disease Nematode Bursaphelenchus xylophilus.";
RL J. Bacteriol. 194:3764-3764(2012).
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:EIC85668.1}.
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DR EMBL; AJHJ01000004; EIC85668.1; -; Genomic_DNA.
DR RefSeq; WP_009635602.1; NZ_AJHJ01000004.1.
DR AlphaFoldDB; I0QWJ5; -.
DR STRING; 932213.SPM24T3_04996; -.
DR PATRIC; fig|932213.3.peg.997; -.
DR eggNOG; COG0612; Bacteria.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000011072; 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; 2.
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; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003632678"
FT DOMAIN 51..162
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 201..295
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 485..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 56531 MW; AD62C10305C066BE CRC64;
MQGTRIRLLL GGLLLASAYS NVQAEALQPD PAWQQGKLDN GFNWQLLTTP QRPNDRIELR
LVVRTGSLAE NPQQQGFAHF LPRLALIRSE GFTTAQLQSF WQQAIDNQRP MSPAVTSYDF
TSYNLSLPNG RPDLIKSALH WLVDTSSKMV VTPDSLHAAW QAPQDPIDSV PSDSGDGWWR
YRIGGSTLVG HSPELLPAKT VKAADLGKFY HQWYTPDVMT LYVVGNVDSR AMAEQIKSAF
ASLKGSRQIP QTMPTLSDVA PKVMSTFDPS LTQDRLSLMW SMPWQPIQDS PALNAYWRSD
LAREALFLHL QQALKTPADS KESKDGGSIQ PALGFDCRVQ YQHAQCAVRM EAPKEAIQPA
LKRLAGELVK VRDNGLSQAE FDALVAQKKD QLGQLFAIYA RTDTGVLMSQ RLRSQQNGVV
DIAPEQYQKL RQAFLSTLTL PDFNQELKQQ LSHDPSMMLV QPKGEAELSV KTLQDTYDSI
VVPTAATPAD APPSTDASQA STSAGSGSST TVQ
//