ID L9LSM1_9GAMM Unreviewed; 1012 AA.
AC L9LSM1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Peptidase M66 {ECO:0000313|EMBL:ELW77724.1};
GN ORFNames=ACINWC743_2397 {ECO:0000313|EMBL:ELW77724.1};
OS Acinetobacter sp. WC-743.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=903945 {ECO:0000313|EMBL:ELW77724.1, ECO:0000313|Proteomes:UP000011515};
RN [1] {ECO:0000313|EMBL:ELW77724.1, ECO:0000313|Proteomes:UP000011515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WC-743 {ECO:0000313|EMBL:ELW77724.1,
RC ECO:0000313|Proteomes:UP000011515};
RA Harkins D.M., Brinkac L.M., Durkin A.S., Beck E., Fedorova N.B., Kim M.,
RA Onuska J., Radune D., DePew J., Koroleva G.I., Singh I., Chahine M.A.,
RA Cash D.M., Huang X.-Z., Nikolich M.P., Nierman W.C., Fouts D.E.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01031};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01031};
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:ELW77724.1}.
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DR EMBL; AMFQ01000142; ELW77724.1; -; Genomic_DNA.
DR RefSeq; WP_009587015.1; NZ_AMFQ01000142.1.
DR AlphaFoldDB; L9LSM1; -.
DR PATRIC; fig|903945.3.peg.4295; -.
DR Proteomes; UP000011515; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR019503; Peptidase_M66_dom.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR022218; TagA_dom.
DR PANTHER; PTHR39540; -; 1.
DR PANTHER; PTHR39540:SF1; DICTOMALLEIN-1-RELATED; 1.
DR Pfam; PF10462; Peptidase_M66; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR Pfam; PF12561; TagA; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51694; PEPTIDASE_M66; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01031};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01031};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01031};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01031}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01031}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1012
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004000366"
FT DOMAIN 326..587
FT /note="Peptidase M66"
FT /evidence="ECO:0000259|PROSITE:PS51694"
FT REGION 24..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 479
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT BINDING 482
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT BINDING 488
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
SQ SEQUENCE 1012 AA; 109418 MW; D45F3DD7C2E3685B CRC64;
MHLRFKYLTI CTLSAMLIAC GGGGESHSVN DQPSNLPQNP GDGTNELPGD GTPEIPDNGS
GGSNNGSTET PPNSGSDGSN NGSIETPPEN GSGGSNNGST ETPPNSGSDG SNNGSTETPP
ENGSGGSNNG STGTPPENGS GGSNNGSEGN TGTTPPTVDK YPEPVKNKIS NKILGFYDFN
GQGENRLLRN DLTGNFAAMV QFVQSHAVNP KNNEQDKMPR LTTEKDALLL VTPLVAMGEL
NQLQAEIYQG NQLIRTVNLK EPSRLAASDQ SNQDDRARVM YSKQAWSLAL KWDEVRPGLT
IRVIDPVNNR SGALGGSDID FAAPGELVVQ SIRLGLLTDA PKSNGHYMLL EPEKAGTDYL
QTIPAAKMIV SKYEEMKLNR VMVASGVIYD SASATNGGVY DGDMRENTAK STFSVGINLA
NWGVTSSSMQ SQEQPQLTQS VVIHHARGKY ANGESNHGLS GGNGILTLID SIGNEFSHEI
GHHYGLGHYP GSVETSGSPT NYFWSAHHAD SGWGYIAFRN KMRGNLNWGS TNLGDGSNGV
PNFQNLYAYG WDAMSGGASA SSISKYTHYT GYSTWLKIQP AFDKYIWDAN SITGYKKWNA
NTREMVDAQP KTPNSGNVWY NSADGNFLKP RLFSVPVYTI LGGYDPVNQV GIVYPAARGN
WGNVFNLPQV NTSSTAASCW LNVQYASKVE HIALAPQRVN AGSNANKFHV NLAQSDAPQN
VDLYCQKTGQ QAVKLSSISI PVAIEAMTPF VTIGKEAEYS ALRKIEMPQL EQALLNNQGK
AVVKLDANSR LLFDSYRLFK TELSPNAQLE MVRYTQQQIK LYRLNRWINA YRVDLESGNA
EAIEAFNRFV AKLELNNDFN LNEVSSLKNG TNCLKVETLS DGKLNAYISG KSACTGDDSE
QWIYDAMGKI HSKKYMDQCL ASQAGVINLA SCNNESSAQA WMINSTLQRI EQGSKCFDLE
YGYLNNNRAR LISYNCGTGG NQKWTSLRSN NSLILAATSS ANLPLIKQLL IH
//
