ID A0A127JY94_9BURK Unreviewed; 495 AA.
AC A0A127JY94;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=UC35_21700 {ECO:0000313|EMBL:AMO24967.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO24967.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO24967.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO24967.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
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; CP010951; AMO24967.1; -; Genomic_DNA.
DR RefSeq; WP_061503383.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127JY94; -.
DR PATRIC; fig|94132.3.peg.4425; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000070433; 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:UP000070433}.
FT DOMAIN 331..338
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 263
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT ACT_SITE 337
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 256
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 333
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ SEQUENCE 495 AA; 51623 MW; 7F82D310AA421777 CRC64;
MDFQLKTLDP ARAAREKCDA IVLVVAQGFK PAKDPLTSLA GHALDAGDLE AKPGKLLHAY
RSEGIAASRV ILAGAGDGSA RRVQSAVQAA VGALRSSGVK RLLICLPGEA DEAAVRAAVT
ATAEASYVYV ATKSKPEGRE IERVTVAVDD AARVKDAFEA AKAAAAGIEF ARELANLPPN
HATPTRLGEE AKKLAKAHGF GCQVLGPKEI AKLGMGSFMA VAQGSEEPPR FIVLQHQGGA
DGEAPVVLVG KGITFDSGGI SIKPAQDMDE MKFDMGGAAS VLGTFRAIGE LKPRVNVVGL
IPSCENMPDG RSVKPGDIVK SMSGQTIEIL NTDAEGRLIL CDALSYAERF KPGAVIDIAT
LTGACMVALG GVRSGLFASD DMLAESLQSA GDAAMDLCWR MPLDDEYGDG LKTNFADVAN
VAGRAGGAIT AAKFLQRFAG KFPWAHLDIA GTAWRSGANK GATGRPVGLL YQYLLSRQDS
APAPTKTRRR ASARQ
//
