ID A0A060QG72_9PROT Unreviewed; 473 AA.
AC A0A060QG72;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase B {ECO:0000313|EMBL:CDG38241.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:CDG38241.1};
GN ORFNames=ASAP_0196 {ECO:0000313|EMBL:CDG38241.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG38241.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG38241.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38241.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24682158; DOI=10.1093/gbe/evu062;
RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT life in insect guts.";
RL Genome Biol. Evol. 6:912-920(2014).
RN [2] {ECO:0000313|EMBL:CDG38241.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG38241.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA Lievens P.M., Daffonchio D., Bandi C.;
RT "Evolution of mitochondria reconstructed from the energy metabolism of
RT living bacteria.";
RL PLoS ONE 9:e96566-e96566(2014).
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:CDG38241.1}.
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DR EMBL; CBLX010000003; CDG38241.1; -; Genomic_DNA.
DR RefSeq; WP_031240560.1; NZ_CBLX010000003.1.
DR AlphaFoldDB; A0A060QG72; -.
DR eggNOG; COG0260; Bacteria.
DR Proteomes; UP000027583; Unassembled WGS sequence.
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:SF53; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 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:CDG38241.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDG38241.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 313..320
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 473 AA; 50118 MW; FC7AEFC03DE66302 CRC64;
MRNPEELCLT TTADAARALH IVPVGQDIEA LLHGHGAALR EMVGEPLAGR LYLVPGAAGV
SHAVYLDDPQ SCDAARFGAL ATGLPSGDWV PAVAPDYAGS RPEIMQDVVM GFCMGAYHYA
IGPASENTVR LVLPPECNTG RAVALAQATW LGRDLVNMPA NLLGPVELAQ RAEAVARLHD
ATSEIVSGEA LERAYPCLAA VGAGSDRPAQ VFRMTWQGST AGADAPLLSL VGKGVCFDTG
GYDIKPASGM LRMKKDMGGA ALMLSLAHVI MAQDLPLRLE LRLGCVENSI SGHAMRPGDI
LTTRTGLTVE VGNTDAEGRL VLSDLLTEAC ESQPDWLLDA ATLTGAARVA LGPDLPALFS
NDPEWSQILL ESGQETGDAM WQLPLWHGYD AWLRRKNAHL GNVTDKPMAG AITAALFLQH
FVEPTVKWAH IDTYAWNDGA RTGRPEGGET LALRALTIAT LRMINERVGS GSA
//
