| Tag | Content |
|---|
| CPLM ID | CPLM-002171 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Aminopeptidase N |
Protein Synonyms/Alias | Alpha-aminoacylpeptide hydrolase |
Gene Name | pepN |
Gene Synonyms/Alias | b0932; JW0915 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 60 | RLNGEDLKLVSVHIN | acetylation | [1] | | 75 | DEPWTAWKEEEGALV | acetylation | [1] | | 144 | VLARFTTKIIADKIK | acetylation | [1] | | 149 | TTKIIADKIKYPFLL | acetylation | [1] | | 151 | KIIADKIKYPFLLSN | acetylation | [1] | | 274 | GLNIFNSKYVLARTD | acetylation | [1] | | 286 | RTDTATDKDYLDIER | acetylation | [1] | | 495 | ELYDNEGKVIPLQKG | acetylation | [1] | | 545 | APVKLEYKWSDQQLT | acetylation | [1] | | 738 | LMQEYDDKWHQNGLV | acetylation | [1] | | 852 | RAALEQLKGLENLSG | acetylation | [1] | | 864 | LSGDLYEKITKALA* | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. |
Sequence Annotation | REGION 261 265 Substrate binding.
ACT_SITE 298 298 Proton acceptor (Probable).
METAL 297 297 Zinc; catalytic.
METAL 301 301 Zinc; catalytic.
METAL 320 320 Zinc; catalytic.
BINDING 121 121 Substrate. |
Keyword | 3D-structure; Aminopeptidase; Cell inner membrane; Cell membrane; Complete proteome; Direct protein sequencing; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 870 AA |
Protein Sequence | MTQQPQAKYR HDYRAPDYQI TDIDLTFDLD AQKTVVTAVS QAVRHGASDA PLRLNGEDLK 60
LVSVHINDEP WTAWKEEEGA LVISNLPERF TLKIINEISP AANTALEGLY QSGDALCTQC 120
EAEGFRHITY YLDRPDVLAR FTTKIIADKI KYPFLLSNGN RVAQGELENG RHWVQWQDPF 180
PKPCYLFALV AGDFDVLRDT FTTRSGREVA LELYVDRGNL DRAPWAMTSL KNSMKWDEER 240
FGLEYDLDIY MIVAVDFFNM GAMENKGLNI FNSKYVLART DTATDKDYLD IERVIGHEYF 300
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRTMRG LQFAEDASPM 360
AHPIRPDMVI EMNNFYTLTV YEKGAEVIRM IHTLLGEENF QKGMQLYFER HDGSAATCDD 420
FVQAMEDASN VDLSHFRRWY SQSGTPIVTV KDDYNPETEQ YTLTISQRTP ATPDQAEKQP 480
LHIPFAIELY DNEGKVIPLQ KGGHPVNSVL NVTQAEQTFV FDNVYFQPVP ALLCEFSAPV 540
KLEYKWSDQQ LTFLMRHARN DFSRWDAAQS LLATYIKLNV ARHQQGQPLS LPVHVADAFR 600
AVLLDEKIDP ALAAEILTLP SVNEMAELFD IIDPIAIAEV REALTRTLAT ELADELLAIY 660
NANYQSEYRV EHEDIAKRTL RNACLRFLAF GETHLADVLV SKQFHEANNM TDALAALSAA 720
VAAQLPCRDA LMQEYDDKWH QNGLVMDKWF ILQATSPAAN VLETVRGLLQ HRSFTMSNPN 780
RIRSLIGAFA GSNPAAFHAE DGSGYLFLVE MLTDLNSRNP QVASRLIEPL IRLKRYDAKR 840
QEKMRAALEQ LKGLENLSGD LYEKITKALA 870 |
Gene Ontology | GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. GO:0004177; F:aminopeptidase activity; IDA:EcoliWiki. GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0043171; P:peptide catabolic process; IGI:EcoliWiki. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |