ID T0P8B3_AERSA Unreviewed; 434 AA.
AC T0P8B3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Peptidase PepB {ECO:0000313|EMBL:ATP09130.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:ATP09130.1};
GN Name=pepB1 {ECO:0000313|EMBL:ATP09130.1};
GN ORFNames=Asalp_19270 {ECO:0000313|EMBL:ATP09130.1};
OS Aeromonas salmonicida subsp. pectinolytica 34mel.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1324960 {ECO:0000313|EMBL:ATP09130.1, ECO:0000313|Proteomes:UP000222916};
RN [1] {ECO:0000313|Proteomes:UP000222916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34mel {ECO:0000313|Proteomes:UP000222916};
RX PubMed=29304740; DOI=10.1186/s12864-017-4301-6;
RA Pfeiffer F., Zamora-Lagos M.A., Blettinger M., Yeroslaviz A., Dahl A.,
RA Gruber S., Habermann B.H.;
RT "The complete and fully assembled genome sequence of Aeromonas salmonicida
RT subsp. pectinolytica and its comparative analysis with other Aeromonas
RT species: investigation of the mobilome in environmental and pathogenic
RT strains.";
RL BMC Genomics 19:20-20(2018).
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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DR EMBL; CP022426; ATP09130.1; -; Genomic_DNA.
DR RefSeq; WP_021140485.1; NZ_CP022426.1.
DR AlphaFoldDB; T0P8B3; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000222916; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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 Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR047620; M17_PepB-like_N.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF20; PEPTIDASE B; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 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:ATP09130.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ATP09130.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 279..286
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 434 AA; 46254 MW; 88AAE41B40123F15 CRC64;
MADMMNVRLS LQAAAAHWGE GAQLSFNGDE TRIHLGAIAQ ENDALRTIQR AARRLESSGI
KRVKLAGDDW DLERRYAFAQ GFYAAKGTRE LDFGPQSESD ARELDALIKA TRWVREVTNG
CPEAIYPMSL AESALLLIRG LGGDQVTARI TAGEALREAG HIGIWSVGRG SEREPVLLEL
DYNPTGDRNA PVVAALVGKG ITFDSGGYSM KSSDNMLPMK SDMGGAAMVT GALALAISRG
LKHRVKLILC CAENLVSGHA FKLGDILTYK NGISVEIQNT DAEGRLVLAD GLMAASDCGA
AYILDAATLT GAAKTALGRD YNAVFALDEV EQQRTLAAAK AEHEKAWALP LEPWHVGQLT
SAFAELGNVA SAEGTAGATT AAAFLSRFVR DEGKGWVHLD LAASYQKSGN DLWATGAKGH
GLRTIARWLQ EVSA
//
