APEA_THEMA
ID APEA_THEMA Reviewed; 451 AA.
AC Q9WYJ9;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable M18 family aminopeptidase 1;
DE EC=3.4.11.-;
GN Name=apeA; OrderedLocusNames=TM_0365;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD35452.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000512; AAD35452.1; ALT_INIT; Genomic_DNA.
DR PIR; E72387; E72387.
DR RefSeq; NP_228176.1; NC_000853.1.
DR RefSeq; WP_004083171.1; NZ_CP011107.1.
DR PDB; 2GLF; X-ray; 2.80 A; A/B/C/D=2-451.
DR PDBsum; 2GLF; -.
DR AlphaFoldDB; Q9WYJ9; -.
DR SMR; Q9WYJ9; -.
DR STRING; 243274.THEMA_02890; -.
DR MEROPS; M18.004; -.
DR EnsemblBacteria; AAD35452; AAD35452; TM_0365.
DR KEGG; tma:TM0365; -.
DR PATRIC; fig|243274.5.peg.370; -.
DR eggNOG; COG1362; Bacteria.
DR InParanoid; Q9WYJ9; -.
DR OMA; GPILKVN; -.
DR EvolutionaryTrace; Q9WYJ9; -.
DR Proteomes; UP000008183; Chromosome.
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..451
FT /note="Probable M18 family aminopeptidase 1"
FT /id="PRO_0000173458"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:2GLF"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 98..109
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 146..157
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2GLF"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 201..214
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 293..304
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 311..319
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 334..339
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:2GLF"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:2GLF"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:2GLF"
FT HELIX 434..450
FT /evidence="ECO:0007829|PDB:2GLF"
SQ SEQUENCE 451 AA; 50381 MW; C2310E30DA36BCD8 CRC64;
MKMERKNVWH HRKKEEIEAF SKEYMEFMSK AKTERMTVKE IKRILDESGF VPLEDFAGDP
MNMTVYAVNR GKAIAAFRVV DDLKRGLNLV VAHIDSPRLD FKPNPLIEDE QIALFKTHYY
GGIKKYHWLS IPLEIHGVLF KNDGTEIEIH IGDKPEDPVF TIPDLLPHLD KEDAKISEKF
KGENLMLIAG TIPLSGEEKE AVKTNVLKIL NEMYGITEED FVSGEIEVVP AFSPREVGMD
RSLIGAYGQD DRICAYTALR ALLSANPEKS IGVIFFDKEE IGSDGNTGAK ARFYLKALRQ
ILKMQGAKDS EFVLDEVLEN TSVISGDVCA AVNPPYKDVH DLHNAPKLGY GVALVKYTGA
RGKYSTNDAH AEFVARVRKV LNEQGVIWQV ATLGKVDQGG GGTIAKFFAE RGSDVIDMGP
ALLGMHSPFE ISSKADLFET YVAYRSLMEK L
