ID A0A154VJN5_9PROT Unreviewed; 497 AA.
AC A0A154VJN5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AUP43_13795 {ECO:0000313|EMBL:KZD01549.1};
OS Oceanibaculum pacificum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Oceanibaculaceae; Oceanibaculum.
OX NCBI_TaxID=580166 {ECO:0000313|EMBL:KZD01549.1, ECO:0000313|Proteomes:UP000076400};
RN [1] {ECO:0000313|EMBL:KZD01549.1, ECO:0000313|Proteomes:UP000076400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A02656 {ECO:0000313|EMBL:KZD01549.1,
RC ECO:0000313|Proteomes:UP000076400};
RA Lu L., Lai Q., Shao Z., Qian P.;
RT "Genome sequence of Oceanibaculum pacificum MCCC 1A02656.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZD01549.1}.
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DR EMBL; LPXN01000156; KZD01549.1; -; Genomic_DNA.
DR RefSeq; WP_067559673.1; NZ_LPXN01000156.1.
DR AlphaFoldDB; A0A154VJN5; -.
DR STRING; 580166.AUP43_13795; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000076400; Unassembled WGS sequence.
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:UP000076400}.
FT DOMAIN 343..350
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 275
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT ACT_SITE 349
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 263
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 268
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 286
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ SEQUENCE 497 AA; 52676 MW; A04FB7C646FFEEB4 CRC64;
MKIGFAKPET PAKGALVVGV MEDSKFGAAA ADLDIRSGGM LTRAMVASRF TGKAHKTVVV
LAPAGVEFSR VVLYGMGKPE DMGPGWAEEM GGNVYAALAS SGETEAALWV EGAEGKAEEL
AVIAAHAAYG ALLRSYRFDK YRTKEKAEDK PTLKKLTVLT DKASTAKKLF GDLEAIAEGV
FLTRDVVSEP GNIIYPETLA DVAKGLTDLG VEVEVLGQKE MKKLGMGALL GVAQGSVREP
KMVIMQWKGA PKSKEAPLAF IGKGVTFDTG GISIKPAGGM EEMKWDMGGS GTVIGLMKAL
AGRKAKANVI GIVGLVENMP DGNAQRPGDI VTSMSGQTIE VINTDAEGRL VLADCLWYCQ
DRFKPRFMVD LATLTGAIII SLGHEHAGMF ASDDGLAEQI AACGKEIGET VWRMPIGDSY
DKELNTDAAD MKNVGGRPGG SITAAMFLKR FTNDVPWVHL DIAGVAWAYK DKPTVPKGAS
GYGVRLLDRL VAVHYEA
//
