ID R9AV32_9GAMM Unreviewed; 897 AA.
AC R9AV32;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Peptidase M66 domain-containing protein {ECO:0000259|PROSITE:PS51694};
GN ORFNames=I593_02703 {ECO:0000313|EMBL:EOR05885.1};
OS Acinetobacter tandoii DSM 14970 = CIP 107469.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1120927 {ECO:0000313|EMBL:EOR05885.1, ECO:0000313|Proteomes:UP000016201};
RN [1] {ECO:0000313|EMBL:EOR05885.1, ECO:0000313|Proteomes:UP000016201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 107469 {ECO:0000313|EMBL:EOR05885.1,
RC ECO:0000313|Proteomes:UP000016201};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter tandoii CIP 107469.";
RL Submitted (MAR-2013) 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:EOR05885.1}.
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DR EMBL; AQFM01000040; EOR05885.1; -; Genomic_DNA.
DR AlphaFoldDB; R9AV32; -.
DR PATRIC; fig|1120927.3.peg.2631; -.
DR eggNOG; ENOG502Z7RH; Bacteria.
DR Proteomes; UP000016201; 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 SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS51694; PEPTIDASE_M66; 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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU01031}.
FT DOMAIN 212..473
FT /note="Peptidase M66"
FT /evidence="ECO:0000259|PROSITE:PS51694"
FT REGION 24..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 365
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT BINDING 364
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01031"
SQ SEQUENCE 897 AA; 98376 MW; 3C7BFFDF1CC234CB CRC64;
MNYHSHVLSV CIASILLSAC GGGGGDSAGG GSKNPDSSVD TAPSEPVYPE PTKDVLDEDT
FGFYDYDATS ATRVIRSDLT GSFQGMVQFA QAHVVDPSGN EAKKMPRLTS EREALLLLTP
TSAMGDIQSL EIEIYQDGLF VRKVKLDDPS QIPLSDQSNQ DQRPQVLYSK RAWSAKLNWN
EVKPGLKLKF VDGSGRVGEL LETQIDFAAP GVLVLNNIRL GLLTDPPVST GHYMLLEPEK
AGTDYFQTIP ASEMIVAKYD DMKLNRVMVA NGTIYDTSSA VEGGVYSGDM RENVAKSTFS
VGINLANWGV TSASMASQEQ PQLTESVIVH HARGQYTNGI QNHGLSGGNG MLTLIDSIGN
EFSHEIGHHY GLGHYPGSVS VEGQPTNYFW SAHHADSGWG YISFRNKMRG NLNWKSTSLG
DGANGVPNFL KLYPYGWDAM AGGATASSIS RYTHYTGYST STKIQPHFNR YIWDANSSTG
YTKWNATTRK MEVVQPRVPS SSKVWYNRTD CNYLKPRLFG VPVYTILGGY DPENQVGLLY
PAARSNWGNV FDLPEANTAV TQAACWLNIR SVSGNKTVGL APNRMDSTNS PANKLHVNLA
ISDQPQHVDL YCKKANQAEK LLSSIDIPTY AEAMRPAVKI GRENGYDALR KIELPNLEQE
LEAQNGKPIV ALSTQNKLLY DSYRTNQEGL SATAQQVLAQ YSDQQQKIYR LNRWMNVYAQ
DLAANNVAAK SALASFIQQL GLETDSLLNQ QSTLLNRTNC LKVEKTTSGQ YNPYISGPTG
CTGDDSEKWI LDGLGRIHSK WAVDQCLTSN GSGGKITLTT CSTQLSSQVW IMAADTQSIR
QGNQCFDLNR GYLVDNRADL IRYSCTNGAN QKWSMLTPNN NLILSYLKPK NLAVLVN
//
