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Database: UniProt
Entry: A0A0K2JI64_SPIKU
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ID   A0A0K2JI64_SPIKU        Unreviewed;       450 AA.
AC   A0A0K2JI64;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Leucyl aminopeptidase {ECO:0000313|EMBL:ALA98269.1};
GN   Name=pepA {ECO:0000313|EMBL:ALA98269.1};
GN   ORFNames=SKUN_001402 {ECO:0000313|EMBL:ALA98269.1};
OS   Spiroplasma kunkelii CR2-3x.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=273035 {ECO:0000313|EMBL:ALA98269.1, ECO:0000313|Proteomes:UP000062963};
RN   [1] {ECO:0000313|EMBL:ALA98269.1, ECO:0000313|Proteomes:UP000062963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CR2-3x {ECO:0000313|EMBL:ALA98269.1,
RC   ECO:0000313|Proteomes:UP000062963};
RX   PubMed=26494665;
RA   Davis R.E., Shao J., Dally E.L., Zhao Y., Gasparich G.E., Gaynor B.J.,
RA   Athey J.C., Harrison N.A., Donofrio N.;
RT   "Complete Genome Sequence of Spiroplasma kunkelii Strain CR2-3x, Causal
RT   Agent of Corn Stunt Disease in Zea mays L.";
RL   Genome Announc. 3:e01216-e01215(2015).
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP010899; ALA98269.1; -; Genomic_DNA.
DR   RefSeq; WP_053391324.1; NZ_CP010899.1.
DR   AlphaFoldDB; A0A0K2JI64; -.
DR   STRING; 273035.SKUN_001402; -.
DR   KEGG; skn:SKUN_001402; -.
DR   PATRIC; fig|273035.7.peg.1731; -.
DR   OrthoDB; 9809354at2; -.
DR   Proteomes; UP000062963; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
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; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR000819; Peptidase_M17_C.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11963:SF23; ZGC:152830; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   PRINTS; PR00481; LAMNOPPTDASE.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00631; CYTOSOL_AP; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:ALA98269.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          304..311
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   450 AA;  49604 MW;  3606A3C28DAE343E CRC64;
     MVLLNDKKQD LTLKAIFKGD KINPLVVQEN GATTLISEEK TIYSYFEKAL TFKNAEDFIQ
     NFMKTIKYSL NIDVDTFKKG AEANTHIFKA LAEGTLYVLN DNYNLKTDKK EKSVYTINLI
     HNCDKAPTIF KEIQIKMECV NFARMLQDTP PNLMYPEVFA EKIKKMAKGI PNLKVTVLDK
     KEIEKEKMGL LLAVNAGSYL EPRVVILEYL GDRSKKEKVG LIGKGITFDS GGYNLKPSTA
     LTGMKFDMSG AAIVCSTVLA LAKAQVKTNI AAVACLTENR IGGKATLTES VITSMNGKTV
     QIDNTDAEGR LVLADGITYA IRKLNVDKLI EASTLTGAIL VALGKWLTGV FANNDGWYEQ
     FAQAASKAHE GIWRMPILEE HSAVMRKTPI ADLTNAESSR FAGSSTAAAF LCEFVEKKPY
     IHLDIAGTAD TKDGRGTGVM IKTLFELFKE
//
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