ID O51096_BORBU Unreviewed; 412 AA.
AC O51096;
DT 01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Aminopeptidase II {ECO:0000313|EMBL:AAC66461.1};
GN OrderedLocusNames=BB_0069 {ECO:0000313|EMBL:AAC66461.1};
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=224326 {ECO:0000313|EMBL:AAC66461.1, ECO:0000313|Proteomes:UP000001807};
RN [1] {ECO:0000313|EMBL:AAC66461.1, ECO:0000313|Proteomes:UP000001807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / B31 / CIP 102532 / DSM 4680
RC {ECO:0000313|Proteomes:UP000001807};
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R., Lathigra R.,
RA White O., Ketchum K.A., Dodson R., Hickey E.K., Gwinn M., Dougherty B.,
RA Tomb J.F., Fleischmann R.D., Richardson D., Peterson J., Kerlavage A.R.,
RA Quackenbush J., Salzberg S., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA Gocayne J., Weidman J., Utterback T., Watthey L., McDonald L., Artiach P.,
RA Bowman C., Garland S., Fuji C., Cotton M.D., Horst K., Roberts K.,
RA Hatch B., Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; AE000783; AAC66461.1; -; Genomic_DNA.
DR PIR; E70108; E70108.
DR RefSeq; NP_212203.1; NC_001318.1.
DR RefSeq; WP_002656022.1; NC_001318.1.
DR AlphaFoldDB; O51096; -.
DR SMR; O51096; -.
DR STRING; 224326.BB_0069; -.
DR PaxDb; 224326-BB_0069; -.
DR EnsemblBacteria; AAC66461; AAC66461; BB_0069.
DR KEGG; bbu:BB_0069; -.
DR PATRIC; fig|224326.49.peg.467; -.
DR HOGENOM; CLU_054346_1_0_12; -.
DR OrthoDB; 9803993at2; -.
DR BRENDA; 3.4.11.10; 902.
DR Proteomes; UP000001807; 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:SF3; AMINOPEPTIDASE AMPS; 1.
DR Pfam; PF02073; Peptidase_M29; 1.
DR PRINTS; PR00919; THERMOPTASE.
DR SUPFAM; SSF144052; Thermophilic metalloprotease-like; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:AAC66461.1}; 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:UP000001807}.
SQ SEQUENCE 412 AA; 46799 MW; 831789C35343F9B4 CRC64;
MEKDLIKYAE LIILKGINLQ KNQCVLIQGS IDNYNFLKIL AKKAYEHGAK YVKLNIKDID
ILKSRLKFSQ EESLKFIPNA EKSFLEEMVQ DKWARINVDD TENFEDLKES IGQKMSIYQK
ALNLASKTLS QAIMSNEIAW CVVCAPGPKW ASKVLNKKEG SQTLEEFFKI QKKILLLDSE
NPIESWESHG EKLHKRCKTL NELNLEKVIF KTEKTNLEVY LLETSLWTGG SEKIKGTEIE
FNANMPTEEV FTTPNYKKTK GIVYATRPVM VLETLIYGMW LKFENGKVVD FGCDDEKQKE
ILKSHIETDI QAKYIGEVAL VDSSSPIYQS NLIFYSTLYD ENASCHIALG AAYPSCLSNE
EDLKTDADKL TYGCNVSLIH TDLMIGSDDL NVIGVDKNGK EYTIIKAGKF AI
//
