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Database: UniProt
Entry: A0A089IKV6_9BACL
LinkDB: A0A089IKV6_9BACL
Original site: A0A089IKV6_9BACL 
ID   A0A089IKV6_9BACL        Unreviewed;       484 AA.
AC   A0A089IKV6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Peptidase M17 {ECO:0000313|EMBL:AIQ24991.1};
GN   ORFNames=H70737_20305 {ECO:0000313|EMBL:AIQ24991.1};
OS   Paenibacillus sp. FSL H7-0737.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ24991.1, ECO:0000313|Proteomes:UP000029519};
RN   [1] {ECO:0000313|EMBL:AIQ24991.1, ECO:0000313|Proteomes:UP000029519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ24991.1,
RC   ECO:0000313|Proteomes:UP000029519};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M17 family.
CC       {ECO:0000256|ARBA:ARBA00009528}.
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DR   EMBL; CP009279; AIQ24991.1; -; Genomic_DNA.
DR   RefSeq; WP_042189912.1; NZ_CP009279.1.
DR   AlphaFoldDB; A0A089IKV6; -.
DR   KEGG; paej:H70737_20305; -.
DR   eggNOG; COG0260; Bacteria.
DR   HOGENOM; CLU_013734_6_0_9; -.
DR   Proteomes; UP000029519; 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; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR011356; Leucine_aapep/pepB.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR000819; Peptidase_M17_C.
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.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029519}.
FT   DOMAIN          47..126
FT                   /note="Peptidase M17 leucyl aminopeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02789"
FT   DOMAIN          168..474
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00883"
SQ   SEQUENCE   484 AA;  52323 MW;  A37EFFA13DD128EC CRC64;
     MNILFDSANV ADTIVYLAYD EESFPFKLGS PHKQCSSVTW LHARTEEESD VLAVGMGKRK
     DITLERIRRA GGAAARAILK EGCSSASLVR LASEAINRNR DISAADELQA WMEGWILGLY
     RFQTYRGTTK VEGSVDLQLQ SIDWPELSSI ELEAVRVSAQ IRAEGAVVAR DLVNEVPGTL
     NPDRFAEWMA EFFDRDDAAL KVHIYRGQEL VELQMNGLLA VGAGSKHAPA LVEIRYKSNP
     ELPMLALVGK GVTFDLGGMN VKTASDISDA RMDMGGAAAV IGAMDILIRK RANVNVTALI
     PVVDNVPDAE AMLPSSVIRY PNGLTVQVAN TDGEGRLIIA DALIHAANIG ATQAIDIATL
     TGNVGAALGL GIAGIWGDAD ITQSLVEIGE RNGERLWPMP LMDEYEADLQ SNYADLRNVS
     TSPFAGAITA ALFIRRFVAE SMSWVHIDMA GTVQYKQDVG YSEAGATGYG ARLLADYVMK
     QVHH
//
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