ID APEH_AERPE Reviewed; 582 AA. AC Q9YBQ2; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Acylamino-acid-releasing enzyme; DE Short=AARE; DE EC=3.4.19.1; DE AltName: Full=Acyl-peptide hydrolase; DE Short=APH; DE AltName: Full=Acylaminoacyl-peptidase; GN OrderedLocusNames=APE_1547.1; OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / OS K1). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_TaxID=272557; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1; RX PubMed=10382966; DOI=10.1093/dnares/6.2.83; RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S., RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.; RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, RT Aeropyrum pernix K1."; RL DNA Res. 6:83-101(1999). RN [2] RP CRYSTALLIZATION. RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1; RX PubMed=12037315; DOI=10.1107/s0907444902005875; RA Wang G., Gao R., Ding Y., Yang H., Cao S., Feng Y., Rao Z.; RT "Crystallization and preliminary crystallographic analysis of acylamino- RT acid releasing enzyme from the hyperthermophilic archaeon Aeropyrum RT pernix."; RL Acta Crystallogr. D 58:1054-1055(2002). CC -!- FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal CC peptide bond of an N-acetylated peptide to generate an N-acetylated CC amino acid and a peptide with a free N-terminus. CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of an N-acetyl or N-formyl amino acid from the N- CC terminus of a polypeptide.; EC=3.4.19.1; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase S9C family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA80546.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000002; BAA80546.2; ALT_INIT; Genomic_DNA. DR PIR; D72636; D72636. DR PDB; 1VE6; X-ray; 2.10 A; A/B=1-582. DR PDB; 1VE7; X-ray; 2.70 A; A/B=1-582. DR PDB; 2HU5; X-ray; 2.00 A; A/B=1-582. DR PDB; 2HU7; X-ray; 2.01 A; A/B=1-582. DR PDB; 2HU8; X-ray; 2.40 A; A/B=1-582. DR PDB; 2QR5; X-ray; 2.20 A; A/B=1-582. DR PDB; 2QZP; X-ray; 2.70 A; A/B=21-582. DR PDB; 3O4G; X-ray; 2.50 A; A/B/C/D=1-582. DR PDB; 3O4H; X-ray; 1.82 A; A/B/C/D=1-582. DR PDB; 3O4I; X-ray; 2.70 A; A/B=1-582. DR PDB; 3O4J; X-ray; 2.50 A; A/B/C/D=1-582. DR PDB; 4RE5; X-ray; 1.90 A; A/B=1-582. DR PDB; 4RE6; X-ray; 2.55 A; A/B/C/D=1-582. DR PDBsum; 1VE6; -. DR PDBsum; 1VE7; -. DR PDBsum; 2HU5; -. DR PDBsum; 2HU7; -. DR PDBsum; 2HU8; -. DR PDBsum; 2QR5; -. DR PDBsum; 2QZP; -. DR PDBsum; 3O4G; -. DR PDBsum; 3O4H; -. DR PDBsum; 3O4I; -. DR PDBsum; 3O4J; -. DR PDBsum; 4RE5; -. DR PDBsum; 4RE6; -. DR AlphaFoldDB; Q9YBQ2; -. DR SMR; Q9YBQ2; -. DR STRING; 272557.APE_1547.1; -. DR ESTHER; aerpe-APE1547; ACPH_Peptidase_S9. DR MEROPS; S09.070; -. DR EnsemblBacteria; BAA80546; BAA80546; APE_1547.1. DR KEGG; ape:APE_1547.1; -. DR eggNOG; arCOG01646; Archaea. DR BRENDA; 3.1.1.1; 171. DR BRENDA; 3.4.19.1; 171. DR EvolutionaryTrace; Q9YBQ2; -. DR Proteomes; UP000002518; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008242; F:omega peptidase activity; IEA:UniProtKB-EC. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR Gene3D; 2.130.10.150; Peptidase/esterase 'gauge' domain; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001375; Peptidase_S9. DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1. DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1. DR Pfam; PF00326; Peptidase_S9; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome. FT CHAIN 1..582 FT /note="Acylamino-acid-releasing enzyme" FT /id="PRO_0000122436" FT ACT_SITE 445 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 524 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT ACT_SITE 556 FT /note="Charge relay system" FT /evidence="ECO:0000250" FT HELIX 9..21 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 24..31 FT /evidence="ECO:0007829|PDB:3O4H" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 35..42 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 45..52 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 65..67 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 90..96 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:4RE5" FT STRAND 111..119 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 124..129 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 143..152 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 163..171 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 174..181 FT /evidence="ECO:0007829|PDB:3O4H" FT TURN 182..184 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 196..202 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 208..213 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 218..223 FT /evidence="ECO:0007829|PDB:3O4H" FT TURN 225..227 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:4RE5" FT HELIX 239..243 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 246..253 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:2QZP" FT STRAND 259..265 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 268..273 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 276..278 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 282..291 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 294..301 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 304..311 FT /evidence="ECO:0007829|PDB:3O4H" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:2QR5" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 324..328 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 330..339 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 345..353 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 358..366 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 368..371 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 380..387 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 391..395 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 401..403 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 405..409 FT /evidence="ECO:0007829|PDB:3O4H" FT TURN 410..413 FT /evidence="ECO:0007829|PDB:3O4H" FT TURN 415..417 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 418..432 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 436..444 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 446..457 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 465..469 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 474..479 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 483..492 FT /evidence="ECO:0007829|PDB:3O4H" FT TURN 493..495 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 497..502 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 505..511 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 516..521 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 525..527 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 529..541 FT /evidence="ECO:0007829|PDB:3O4H" FT STRAND 546..551 FT /evidence="ECO:0007829|PDB:3O4H" FT HELIX 561..579 FT /evidence="ECO:0007829|PDB:3O4H" SQ SEQUENCE 582 AA; 63035 MW; A9F2DD39ACD1C3DF CRC64; MRIIMPVEFS RIVRDVERLI AVEKYSLQGV VDGDKLLVVG FSEGSVNAYL YDGGETVKLN REPINSVLDP HYGVGRVILV RDVSKGAEQH ALFKVNTSRP GEEQRLEAVK PMRILSGVDT GEAVVFTGAT EDRVALYALD GGGLRELARL PGFGFVSDIR GDLIAGLGFF GGGRVSLFTS NLSSGGLRVF DSGEGSFSSA SISPGMKVTA GLETAREARL VTVDPRDGSV EDLELPSKDF SSYRPTAITW LGYLPDGRLA VVARREGRSA VFIDGERVEA PQGNHGRVVL WRGKLVTSHT SLSTPPRIVS LPSGEPLLEG GLPEDLRRSI AGSRLVWVES FDGSRVPTYV LESGRAPTPG PTVVLVHGGP FAEDSDSWDT FAASLAAAGF HVVMPNYRGS TGYGEEWRLK IIGDPCGGEL EDVSAAARWA RESGLASELY IMGYSYGGYM TLCALTMKPG LFKAGVAGAS VVDWEEMYEL SDAAFRNFIE QLTGGSREIM RSRSPINHVD RIKEPLALIH PQNDSRTPLK PLLRLMGELL ARGKTFEAHI IPDAGHAINT MEDAVKILLP AVFFLATQRE RR //