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Database: UniProt
Entry: K2AZ89_9BACT
LinkDB: K2AZ89_9BACT
Original site: K2AZ89_9BACT 
ID   K2AZ89_9BACT            Unreviewed;       460 AA.
AC   K2AZ89;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Cytosol aminopeptidase domain-containing protein {ECO:0000259|PROSITE:PS00631};
GN   ORFNames=ACD_60C00029G0011 {ECO:0000313|EMBL:EKD54984.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD54984.1};
RN   [1] {ECO:0000313|EMBL:EKD54984.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKD54984.1}.
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DR   EMBL; AMFJ01025354; EKD54984.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2AZ89; -.
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; IPR048816; Peptidase_M17_N_1.
DR   PANTHER; PTHR11963:SF53; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR   Pfam; PF00883; Peptidase_M17; 1.
DR   Pfam; PF21337; Peptidase_M17_N_1; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          303..310
FT                   /note="Cytosol aminopeptidase"
FT                   /evidence="ECO:0000259|PROSITE:PS00631"
SQ   SEQUENCE   460 AA;  50422 MW;  755E565B0A629CC0 CRC64;
     MLKCFTTNTQ KAIPIKVITP IDFPAWLKKQ NAMTKNWLTS SGFQLTAGKF SLLPDAAGNI
     TQVLFGTDDI KNFWSIGNLP VILPEGKYIF DIPEEYYAHY GIAFGLGAYQ FTRYKKPLKG
     SAELVLLKND DFSFIENTVE SIYWVRDLIN TPTDDMGPTE FASAAVSFAK QYGASIKQIV
     GDDLLKKNFP CIHTVGRASD DEPRLLDLRW GNPKHPKVTL VGKGVCFDTG GLDIKPSSSM
     LLMKKDMAGA AHVLGLARMV IEATLPISLR VLIPVVENAI SGNAFRPGDI ITSRKGITIE
     IGNTDAEGRL VLADALTEAV SEKPDLVIDI STLTGAARVA VGTDISLMFS NQDDLALNVI
     RHGDQQQDPI CRLPLFAGYR EALNSSIADI NNAAMDSYAG AITAALFLKE FVPNDIPWLH
     FDIMAWNLKS KPGHPQGGEA MGLRALFSYL RERYSRQNGC
//
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