ID A0A0X1TK48_9FIRM Unreviewed; 486 AA.
AC A0A0X1TK48;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
DE EC=3.4.11.1 {ECO:0000256|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
DE Short=LAP {ECO:0000256|HAMAP-Rule:MF_00181};
DE EC=3.4.11.10 {ECO:0000256|HAMAP-Rule:MF_00181};
DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181};
GN Name=pepA {ECO:0000256|HAMAP-Rule:MF_00181};
GN ORFNames=AT726_05715 {ECO:0000313|EMBL:AMC08468.1};
OS Turicibacter sp. H121.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Turicibacteraceae; Turicibacter.
OX NCBI_TaxID=1712675 {ECO:0000313|EMBL:AMC08468.1, ECO:0000313|Proteomes:UP000057144};
RN [1] {ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|Proteomes:UP000057144};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMC08468.1, ECO:0000313|Proteomes:UP000057144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H121 {ECO:0000313|EMBL:AMC08468.1,
RC ECO:0000313|Proteomes:UP000057144};
RX PubMed=27013036;
RA Auchtung T.A., Holder M.E., Gesell J.R., Ajami N.J., Duarte R.T., Itoh K.,
RA Caspi R.R., Petrosino J.F., Horai R., Zarate-Blades C.R.;
RT "Complete Genome Sequence of Turicibacter sp. Strain H121, Isolated from
RT the Feces of a Contaminated Germ-Free Mouse.";
RL Genome Announc. 4:0-0(2016).
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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000135, ECO:0000256|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:0000256|ARBA:ARBA00000967, ECO:0000256|HAMAP-
CC Rule:MF_00181};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00181};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-Rule:MF_00181}.
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DR EMBL; CP013476; AMC08468.1; -; Genomic_DNA.
DR RefSeq; WP_055276657.1; NZ_JAMQUX010000001.1.
DR AlphaFoldDB; A0A0X1TK48; -.
DR STRING; 1712675.AT726_05715; -.
DR KEGG; tur:AT726_05715; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000057144; 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; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 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; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW Rule:MF_00181}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00181};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00181};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00181};
KW Reference proteome {ECO:0000313|Proteomes:UP000057144}.
FT DOMAIN 334..341
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 266
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT ACT_SITE 340
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 259
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 336
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ SEQUENCE 486 AA; 52479 MW; E20BD29EE2D5FA59 CRC64;
MIEFKSSLKI KNEKTNLVVG VFSDISHDII TQLDKALNKR LSVSLEEGLI PTNFKDITPI
YPLGQIESKK VYIVGLGKST DFTVEKCRKV LGKVAKAAKE DVTILLETFD CKAVSINELA
TVCAEAITLS TYKMETYKTE EKATTPVNFF IHCDSQITDD LNRGVIYGEA TNSARQLLNE
PGNKLTATDL ASHIAQFANE HELEIRIVEK DEMEQLGMGG ILGVNRGSVQ PPKMIVVKYQ
GTPRFENITA LVGKGLTFDT GGYCLKPRSG MEAMKGDMGG AASAFGAFQV AVRLNLPVNL
LLVIPSTDNM ISGDAIKPGD ILTTMSGKTV EVTNTDAEGR LILADGITFA KHLGASKIID
LATLTGAIIA ALGADTTGAF TNNQAFLDEF QKAADLTNEY MWQMPLFPRD QKALRNSDVA
DLNNAPIGKP GAIMAAAFLK EFVEDTPWIH LDIAGTADSK TAYDLGPKGG TGVMVRTIAK
YLELQG
//
