AMPA_XANOR
ID AMPA_XANOR Reviewed; 490 AA.
AC Q5H4N2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
DE Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181};
DE EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181};
GN Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181}; OrderedLocusNames=XOO0834;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
CC -!- FUNCTION: Presumably involved in the processing and regular turnover of
CC intracellular proteins. Catalyzes the removal of unsubstituted N-
CC terminal amino acids from various peptides. {ECO:0000255|HAMAP-
CC Rule:MF_00181}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00181};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, preferentially leucine,
CC but not glutamic or aspartic acids.; EC=3.4.11.10;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00181};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP-
CC Rule:MF_00181}.
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DR EMBL; AE013598; AAW74088.1; -; Genomic_DNA.
DR RefSeq; WP_011257713.1; NC_006834.1.
DR PDB; 3JRU; X-ray; 2.60 A; A/B=1-490.
DR PDBsum; 3JRU; -.
DR AlphaFoldDB; Q5H4N2; -.
DR SMR; Q5H4N2; -.
DR STRING; 291331.XOO0834; -.
DR MEROPS; M17.003; -.
DR EnsemblBacteria; AAW74088; AAW74088; XOO0834.
DR KEGG; xoo:XOO0834; -.
DR PATRIC; fig|291331.8.peg.932; -.
DR HOGENOM; CLU_013734_0_1_6; -.
DR OMA; MKNTGPR; -.
DR BRENDA; 3.4.11.1; 6717.
DR Proteomes; UP000006735; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Protease; Reference proteome.
FT CHAIN 1..490
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_1000020002"
FT ACT_SITE 274
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT ACT_SITE 348
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 267
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 267
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 285
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 344
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3JRU"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 44..50
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 88..102
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 166..187
FT /evidence="ECO:0007829|PDB:3JRU"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 242..249
FT /evidence="ECO:0007829|PDB:3JRU"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 305..317
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 347..358
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:3JRU"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 392..404
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 416..422
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 438..447
FT /evidence="ECO:0007829|PDB:3JRU"
FT STRAND 455..459
FT /evidence="ECO:0007829|PDB:3JRU"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:3JRU"
FT HELIX 478..489
FT /evidence="ECO:0007829|PDB:3JRU"
SQ SEQUENCE 490 AA; 51035 MW; E7C69495308F7B9F CRC64;
MALQFTLNQD APASAAVDCI VVGAFADKTL SPAAQALDSA SQGRLTALLA RGDVAGKTGS
TTLLHDLPGV AAPRVLVVGL GDAGKFGVAP YLKAIGDATR ALKTGAVGTA LLTLTELTVK
ARDAAWNIRQ AVTVSDHAAY RYTATLGKKK VDETGLTTLA IAGDDARALA VGVATAEGVE
FARELGNLPP NYCTPAYLAD TAAAFAGKFP GAEAEILDEA QMEALGMGSL LSVARGSANR
PRLIVLKWNG GGDARPYVLV GKGITFDTGG VNLKTQGGIE EMKYDMCGGA TVIGTFVATV
KAELPINLVV VVPAVENAID GNAYRPSDVI TSMSGKTIEV GNTDAEGRLI LCDALTYAER
FNPEALVDVA TLTGACMVAL GHQTAGLMSK HDDLANELLA AGEHVFDRAW RLPLWDEYQG
LLDSTFADVY NIGGRWGGAI TAGCFLSRFT ENQRWAHLDI AGVASDEGKR GMATGRPVGL
LTQWLLDRAA
