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Database: UniProt
Entry: A0A1S8CRQ3_9GAMM
LinkDB: A0A1S8CRQ3_9GAMM
Original site: A0A1S8CRQ3_9GAMM 
ID   A0A1S8CRQ3_9GAMM        Unreviewed;       500 AA.
AC   A0A1S8CRQ3;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=BKE30_13530 {ECO:0000313|EMBL:ONG37915.1};
OS   Alkanindiges hydrocarboniclasticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Alkanindiges.
OX   NCBI_TaxID=1907941 {ECO:0000313|EMBL:ONG37915.1, ECO:0000313|Proteomes:UP000192132};
RN   [1] {ECO:0000313|EMBL:ONG37915.1, ECO:0000313|Proteomes:UP000192132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H1 {ECO:0000313|EMBL:ONG37915.1,
RC   ECO:0000313|Proteomes:UP000192132};
RA   Subhash Y., Lee S.;
RT   "Draft Genome sequence of Alkanindiges sp. strain H1.";
RL   Submitted (OCT-2016) 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:ONG37915.1}.
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DR   EMBL; MLCN01000042; ONG37915.1; -; Genomic_DNA.
DR   RefSeq; WP_076879133.1; NZ_MLCN01000042.1.
DR   AlphaFoldDB; A0A1S8CRQ3; -.
DR   STRING; 1907941.BKE30_13530; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000192132; 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:SF23; CYTOSOL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 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}.
FT   DOMAIN          350..357
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         270
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         275
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         293
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
FT   BINDING         354
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00181"
SQ   SEQUENCE   500 AA;  53901 MW;  1A43119B2E091FB5 CRC64;
     MKLNLQNKLL PTSDTTADSA SSANATLVLV LDQETLVQAH DQLPDDVQQQ LATHIERAQF
     KAKLGETLPI YQLNNTDFSQ VLLVGAGELN KMTAGQAQTL AGSIYKALAN RTAQAVISLD
     ALADLHIDTF VLALSNAAYR FDTYKSKKSE AILDSITLHS TRADELKSRI DYLQAVAKGQ
     SLARDVGNQP ANVCHPEYMA EQALQLAQQY PDLLKVTVLD EAAMQELGMN ALLAVSHGSE
     REARLVVMEY QGKSDNFQSD QGKPVVLVGK GITFDTGGIS MKPAAGMDEM KFDMCGAASV
     LGTLQALCEA KLPVNVVGTL VCAENMPSGR ATRPGDIVTT MSGQTVEILN TDAEGRLVLC
     DALTYIKRFN PDTVIDIATL TGACVVALGK VLAGLFSPDN ELASELQQAG QLSHDRVWRM
     PVIDDYQELL DSPFADMGNI GGPYGGAITA ACFLQRFTRE YRWAHLDIAG VAWLSGTHKG
     ATGRPVPLLM QFLRNRSQAS
//
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