AMPA_SULSY
ID AMPA_SULSY Reviewed; 504 AA.
AC B2V6F5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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};
GN OrderedLocusNames=SYO3AOP1_0038;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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; CP001080; ACD65687.1; -; Genomic_DNA.
DR RefSeq; WP_012458779.1; NC_010730.1.
DR AlphaFoldDB; B2V6F5; -.
DR SMR; B2V6F5; -.
DR STRING; 436114.SYO3AOP1_0038; -.
DR MEROPS; M17.016; -.
DR EnsemblBacteria; ACD65687; ACD65687; SYO3AOP1_0038.
DR KEGG; sul:SYO3AOP1_0038; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_2_2_0; -.
DR OMA; MKNTGPR; -.
DR OrthoDB; 356206at2; -.
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 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease.
FT CHAIN 1..504
FT /note="Probable cytosol aminopeptidase"
FT /id="PRO_1000098355"
FT ACT_SITE 275
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT ACT_SITE 349
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181"
SQ SEQUENCE 504 AA; 56325 MW; 096FA6928D9151E2 CRC64;
MEINLTTKKL DNVKTDAVFF LMFEDNKKLE GELEKIDKAL NGGVSDLIKL QKYKAEEGKF
LIVPTLGKIK ANYVAIVGLG KEKKFENDIL RRVASYIIRK AKELKLSDII IDTNLQQFEN
YDEVVQAITE GLILGDYSFD KYFSKKDEHK VKEVQVNIPK NQDKDRLNEF VRIGEILAEA
QNFTRDLVNE PANVINTIQF AEIAEKLAKE YGFEIKIYDE EEIEKMGMGA YLAVAKGSDN
PPRFIHLTYR PKNSQGEVAI VGKGLMFDSG GLNIKTGDFM RWMKSDKSGA CAVFGIFKAI
GELKPDITVH GIVAAAENMP SGKAYRPDDI LKAKNGVTIE VGNTDAEGRL TLADALSYAS
ELKPDAIIDM ATLTGACVVA LGEFTAGVMG NNQKFINEIL KTSEETGEWM WQLPFNDKLR
EQIKAPHADV YNVGTTRYGG AITAGLFLEK FVDPKIPWVH IDIAGPSHHT SGWYYHPKGA
TGIPVRTITW YLLKRSKFFD KIGK
