ID F3Z2F9_DESAF Unreviewed; 399 AA.
AC F3Z2F9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Peptidase M29 aminopeptidase II {ECO:0000313|EMBL:EGJ51292.1};
GN ORFNames=Desaf_2990 {ECO:0000313|EMBL:EGJ51292.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ51292.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ51292.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ51292.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M29 family.
CC {ECO:0000256|ARBA:ARBA00008236}.
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DR EMBL; CP003221; EGJ51292.1; -; Genomic_DNA.
DR RefSeq; WP_014260945.1; NC_016629.1.
DR AlphaFoldDB; F3Z2F9; -.
DR STRING; 690850.Desaf_2990; -.
DR KEGG; daf:Desaf_2990; -.
DR eggNOG; COG2309; Bacteria.
DR HOGENOM; CLU_057697_0_0_7; -.
DR Proteomes; UP000007844; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1830.10; Thermophilic metalloprotease (M29); 1.
DR InterPro; IPR035097; M29_N-terminal.
DR InterPro; IPR000787; Peptidase_M29.
DR PANTHER; PTHR34448; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR34448:SF1; BLL6088 PROTEIN; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:EGJ51292.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007844}.
SQ SEQUENCE 399 AA; 45263 MW; EC76765CBD7E58F5 CRC64;
MFDSMRLEKY ADVLIWGLKT SRKKPFANGD VVLVRFDAPA LPLVEALYGK LLDMRLNPVV
RLQPTAGMER SFYDLSGQKQ LTFVPPGEKE LVDNLSGLVS ILAPQSLTHL SHVDPASFGM
FQKSRKFLRD IMDRREEQGE FGWTLCLYPT PALAEKAGLS IEEYARQIEK ACYLNMAQPE
QDWQQFWNAA QEIKAKLNSL DIESYHIESE RTDLRVVGGL MRRWVGITGH NIPSFEMYIS
PDWRGTEGVF YADLPSYRSG NYIKGVKLTF KAGVVTDVQA EQGQEFTIQQ LNMDQGARRL
GEFSLTDRRF SRIDRFMAHT LYDENFGGQN GNCHVAVGSS YSDTYAGDPA ELTLERKEEL
GFNNSALHWD LINTEAKRVT AYLRGGGKTV IYEQGMFTL
//
