ID K9TUZ8_CHRTP Unreviewed; 863 AA.
AC K9TUZ8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=Chro_0458 {ECO:0000313|EMBL:AFY86006.1};
OS Chroococcidiopsis thermalis (strain PCC 7203).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Chroococcidiopsidaceae; Chroococcidiopsis.
OX NCBI_TaxID=251229 {ECO:0000313|EMBL:AFY86006.1, ECO:0000313|Proteomes:UP000010384};
RN [1] {ECO:0000313|EMBL:AFY86006.1, ECO:0000313|Proteomes:UP000010384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7203 {ECO:0000313|EMBL:AFY86006.1,
RC ECO:0000313|Proteomes:UP000010384};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Chroococcidiopsis thermalis PCC 7203.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; CP003597; AFY86006.1; -; Genomic_DNA.
DR RefSeq; WP_015152557.1; NC_019695.1.
DR AlphaFoldDB; K9TUZ8; -.
DR STRING; 251229.Chro_0458; -.
DR KEGG; cthe:Chro_0458; -.
DR PATRIC; fig|251229.3.peg.539; -.
DR eggNOG; COG0308; Bacteria.
DR eggNOG; COG1413; Bacteria.
DR HOGENOM; CLU_014298_0_1_3; -.
DR InParanoid; K9TUZ8; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000010384; Chromosome.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09603; M1_APN_like; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF13646; HEAT_2; 2.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM00567; EZ_HEAT; 5.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:AFY86006.1};
KW Antenna complex {ECO:0000256|ARBA:ARBA00022549};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Phycobilisome {ECO:0000256|ARBA:ARBA00022738};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000010384};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 26..209
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 244..454
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 826..860
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 863 AA; 97672 MW; 48F2BAEE2132B0D1 CRC64;
MLQSYFDTDN NGHKHKSFEL PGAKPHYNPD RPGQVEHIFL DLNLDIPNQS YDGTCTIQLK
PVRNGIDRLT LDAVSLNIHS VQVDATSTTY DYDGQQLQVH LANPTQTGQS IKIAIAYSVT
KPQRGIYFIA PDKHYPNKPV QVWTQGEDED SRFWFPCFDY PGQLATSEIR VRVPKPYIAI
SNGRLIDTEE NSDYKIFHWL QEQVHPSYLM TLAVGDFAEI QDEWNGKLVT YYVEKGREED
ARRSMGKTPR MVEFFSQKYG YPYAFPKYAQ VCVDDFIFGG MENTSTTLLT DRCLLDERAA
IDNRLTESLV AHELAHQWFG DLVVIKHWSH AWIKEGMASY SEVMWTEQEY GAEDAAYYRL
LEARNYLAED SSRYRRPIVT HVYREAIELY DRHLYEKGSC VYHMIRAELE EELFWRAIQT
FVQDNAHHTV ETVDLLRAIE KVTGRNLLFL FDQYVYRGGH PEFKVAYTWD GDSKLAKVTV
NQTQNDLFDL KIPIAFGYAQ GDVGAHSHAP LHKTFTVRVN EKEQSFYFPL NEKPQFISFD
ANNNYLKTVS LEYSIPELKA QLQFDPDPIS RIYAAEALGK KGGLEALNAL AEALKSDRFW
GVKVEVAKQL AQIKLDQAFE ALVVGLNDEN PLVRRAVVEA LSNIKTYASY KALKPIVEDG
DSSYYVEAAA ARAVGIIAAA QLEEKPKEEK VLKLLRSILE NKAGWNEVVR SGAIAGLSQM
KTSAETLDLI LEYTRLGVPQ ALRLAAVRAL GTISTGQSAA NLDRILERLT ELSHESFFLT
QVSVVTALGQ METPKAIAIL QALATQSLDG RVQRIAEEAV AKVQSAAGSD QAVKQLRDEI
DQLKKQNQTL MSRLESLEAK ASK
//
