ID   W1X6S2_ECOLX            Unreviewed;       498 AA.
AC   W1X6S2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Protein yhjJ {ECO:0000313|EMBL:ETJ25145.1};
GN   ORFNames=Q609_ECAC01313G0005 {ECO:0000313|EMBL:ETJ25145.1};
OS   Escherichia coli DORA_A_5_14_21.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1403943 {ECO:0000313|EMBL:ETJ25145.1, ECO:0000313|Proteomes:UP000018853};
RN   [1] {ECO:0000313|EMBL:ETJ25145.1, ECO:0000313|Proteomes:UP000018853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DORA_A_5_14_21 {ECO:0000313|Proteomes:UP000018853};
RA   Brown C.T., Sharon I., Thomas B.C., Castelle C.J., Morowitz M.J.,
RA   Banfield J.F.;
RT   "A Varibaculum cambriense genome reconstructed from a premature infant gut
RT   community with otherwise low bacterial novelty that shifts toward anaerobic
RT   metabolism during the third week of life.";
RL   Submitted (DEC-2013) 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:ETJ25145.1}.
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DR   EMBL; AZLZ01001313; ETJ25145.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1X6S2; -.
DR   PATRIC; fig|1403943.3.peg.1330; -.
DR   Proteomes; UP000018853; 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; 2.
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..498
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004811649"
FT   DOMAIN          46..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          200..377
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   498 AA;  55456 MW;  9CE0D8395A051B97 CRC64;
     MQGTKIRLLA GGLLMMATAG YVQADALQPD PAWQQGTLSN GLQWQVLTTP QRPSDRVEIR
     LLVNTGSLAE STQQSGYSHA IPRIALTQSG GLEAAQARSL WQQGIDPKRP MPPVIVSYDT
     TLFNLSLPNN RNDLLKEALS YLANATGKLT ITPETINHAL QSQDMVATWP ADTKEGWWRY
     RLKGSTLLGH DPADPLKQPV EAEKIKDFYQ KWYTPDAMTL LVVGNVDARS VVDQINKTFG
     ELKGKRETPA PVPTLSPLRA EAVSIMTDAV RQDRLSIMWD TPWQPIRESA ALLRYWRADL
     AREALFWHVQ QALSASNSKD IGLGFDCRVL YLRAQCAINI ESPNDKLSSN LNLVARELAK
     VRDKGLPEEE FNALVAQKKL ELQKLFAAYA RADTDILMGQ RMRSLQNQVV DIAPEQYQKL
     RQDFLNSLTV EMLNQDLRQQ LSNDMALILL QPKGEPEFNM KALQAAWDQI MAPSTAAAAT
     SVATDDVHPE VTDIPPAQ
//