ID E1IT76_ECOLX Unreviewed; 498 AA.
AC E1IT76;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:EFO57488.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:EFO57488.1};
GN ORFNames=HMPREF9348_03386 {ECO:0000313|EMBL:EFO57488.1};
OS Escherichia coli MS 145-7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679204 {ECO:0000313|EMBL:EFO57488.1, ECO:0000313|Proteomes:UP000003691};
RN [1] {ECO:0000313|EMBL:EFO57488.1, ECO:0000313|Proteomes:UP000003691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 145-7 {ECO:0000313|EMBL:EFO57488.1,
RC ECO:0000313|Proteomes:UP000003691};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2010) 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:EFO57488.1}.
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DR EMBL; ADWS01000018; EFO57488.1; -; Genomic_DNA.
DR RefSeq; WP_001163140.1; NZ_ADWS01000018.1.
DR AlphaFoldDB; E1IT76; -.
DR Proteomes; UP000003691; 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, ECO:0000313|EMBL:EFO57488.1};
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_5003147275"
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; 55529 MW; B4BAE476A83B50A3 CRC64;
MQGTKIRLLA GGLLMMATAG YVQADALQPD PAWQQGTLSN GLQWQVLTTP QRPSDRVEIR
LLVNTGSLAE STQQSGYSHA IPRIALTQSG GLDAAQARSL WQQGIDPKRP MPPVIVSYDT
TLFNLSLPNN RNDLLKEALS YLANATGKLT ITPETINHAL QSQDMVATWP ADTKEGWWRY
RLKGSTLLGH DPADPLKQPV EAEKIKDFYQ KWYTPDAMTL LVVGNVDARS VVDQINKTFG
ELKGKRETPA PVPTLSPLRA EAVSIMTDAV RQDRLSIMWD TPWQPIRESA ALLRYWRADL
AREALFWHVQ QALSASNSKD IGLGFDCRVL YLRAQCAINI ESPNDKLNSN LNLVARELAK
VRDKGLPEEE FNALVAQKKL ELQKLFAAYA RADTDILMGQ RMRSLQNQVV DIAPEQYQKL
RQDFLNSLTV EMLNQDLRQQ LSNDMALILL QPKGEPEFNM KALQAAWDQI MAPSTTAATT
SVATDDVHPE VTDIPPAQ
//
