APEA_BORBU
ID APEA_BORBU Reviewed; 458 AA.
AC P0C925; Q45055;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable M18 family aminopeptidase 1;
DE EC=3.4.11.-;
GN Name=apeA; OrderedLocusNames=BB_0366;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA 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=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
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DR EMBL; AE000783; AAC66747.1; -; Genomic_DNA.
DR PIR; E70145; E70145.
DR RefSeq; NP_212500.1; NC_001318.1.
DR RefSeq; WP_002657823.1; NC_001318.1.
DR PDB; 1Y7E; X-ray; 3.20 A; A=1-458.
DR PDBsum; 1Y7E; -.
DR AlphaFoldDB; P0C925; -.
DR SMR; P0C925; -.
DR STRING; 224326.BB_0366; -.
DR EnsemblBacteria; AAC66747; AAC66747; BB_0366.
DR GeneID; 56567794; -.
DR KEGG; bbu:BB_0366; -.
DR PATRIC; fig|224326.49.peg.761; -.
DR HOGENOM; CLU_590123_0_0_12; -.
DR OMA; GPILKVN; -.
DR EvolutionaryTrace; P0C925; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.250.10; -; 1.
DR HAMAP; MF_00466; Aminopeptidase_M18_1; 1.
DR InterPro; IPR022983; M18_aminopeptidase_1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..458
FT /note="Probable M18 family aminopeptidase 1"
FT /id="PRO_0000173456"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 12..31
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:1Y7E"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:1Y7E"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1Y7E"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 248..253
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 254..267
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 300..312
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 320..328
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 410..416
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 422..426
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1Y7E"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:1Y7E"
FT HELIX 442..454
FT /evidence="ECO:0007829|PDB:1Y7E"
FT TURN 455..457
FT /evidence="ECO:0007829|PDB:1Y7E"
SQ SEQUENCE 458 AA; 51500 MW; 521BC6DAEF0ABA45 CRC64;
MKKQNPWIYL NEEEKNQILN FSESYKKFIS KFKTEREVTA YALDKAKKLG FINAEEKKNL
MPGDKIFYTC REKSVAFAII GKNPIEDGMN FIVSHTDSPR LDAKPSPISE ENELTFIKTN
YYGGIKKYQW LSTPLSIRGV VFLKNGEKVE INIGDNENDP VFVIPDILPH LDRKIQRNKK
SDEIVEGENL KILIGSLPIE TKEKNKVKLA TLQLIKEKYK IEEEDFVSSE IEIVPAGTAK
DVGFDKALIG AYGQDDKICV FTSLESIFDL EETPNKTAIC FLVDKEEIGS TGSTGLDSRY
LEYFVSDMIF KIKKSEYNNL HVQKALWNSK SISADVCAAI NPLFSSVHDE QNAPQLGYGI
PIMKYTGHGG KSMASDADAE LVSYIRQLLN KNNIAWQVAT LGKVEEGGGG TVAKFLAGYG
IRTIDMGPAV ISMHSPMEIT SKFDLYNAYL AYKAFYRE
