APEA_CLOAB
ID APEA_CLOAB Reviewed; 465 AA.
AC Q97K30;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable M18 family aminopeptidase 1;
DE EC=3.4.11.-;
GN Name=apeA; OrderedLocusNames=CA_C1091;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79065.1; -; Genomic_DNA.
DR PIR; F97034; F97034.
DR RefSeq; NP_347725.1; NC_003030.1.
DR RefSeq; WP_010964406.1; NC_003030.1.
DR PDB; 2GLJ; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=5-465.
DR PDBsum; 2GLJ; -.
DR AlphaFoldDB; Q97K30; -.
DR SMR; Q97K30; -.
DR STRING; 272562.CA_C1091; -.
DR EnsemblBacteria; AAK79065; AAK79065; CA_C1091.
DR GeneID; 44997603; -.
DR KEGG; cac:CA_C1091; -.
DR PATRIC; fig|272562.8.peg.1299; -.
DR eggNOG; COG1362; Bacteria.
DR HOGENOM; CLU_590123_0_0_9; -.
DR OMA; GPILKVN; -.
DR OrthoDB; 304020at2; -.
DR EvolutionaryTrace; Q97K30; -.
DR Proteomes; UP000000814; 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..465
FT /note="Probable M18 family aminopeptidase 1"
FT /id="PRO_0000173457"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 20..26
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:2GLJ"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2GLJ"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 264..278
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:2GLJ"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 344..346
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 386..398
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 408..414
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 420..424
FT /evidence="ECO:0007829|PDB:2GLJ"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:2GLJ"
FT STRAND 442..448
FT /evidence="ECO:0007829|PDB:2GLJ"
FT HELIX 449..460
FT /evidence="ECO:0007829|PDB:2GLJ"
SQ SEQUENCE 465 AA; 52011 MW; CB4C6D0A54C0A439 CRC64;
MPNDLLKEYK NAWDKYDDKQ LKEVFALGDR FKNFISNCKT ERECVTELIK TAEKSGYRNI
EDILAKGETL KEGDKVYANN RGKGLIMFLI GKEPLYTGFK ILGAHIDSPR LDLKQNPLYE
DTDLAMLETH YYGGIKKYQW VTLPLAIHGV IVKKDGTIVN VCVGEDDNDP VFGVSDILVH
LASEQLEKKA SKVIEGEDLN ILIGSIPLKD GEEKQKVKHN IMKILNEKYD ISEEDFVSAE
LEIVPAGKAR DYGFDRSMVM GYGQDDRICA YTSFEAMLEM KNAKKTCITI LVDKEEVGSI
GATGMQSKFF ENTVADIMSL CGDYDELKLR KALYNSEMLS SDVSAAFDPN YPNVMEKRNS
AYLGKGIVFN KYTGSRGKSG CNDANPEYIA ELRRILSKES VNWQTAELGK VDQGGGGTIA
YILAEYGMQV IDCGVALLNM HAPWEISSKA DIYETKNGYS AFLNN
