(data stored in ACNUC6774 zone)

HOGENOM: CAMFF_1_PE1011

ID   CAMFF_1_PE1011                       STANDARD;      PRT;   798 AA.
AC   CAMFF_1_PE1011; A0RPT8;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=ATP-dependent protease La; EC=3.4.21 53; (CAMFF_1.PE1011).
GN   Name=lon; OrderedLocusNames=CFF8240_1060;
OS   CAMPYLOBACTER FETUS SUBSP. FETUS 82-40.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=360106;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAMFF_1.PE1011.
CC       Campylobacter fetus subsp. fetus 82-40, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:A0RPT8_CAMFF
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family.
CC   -!- GENE_FAMILY: HOG000261410 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A0RPT8; -.
DR   EMBL; CP000487; ABK81794.1; -; Genomic_DNA.
DR   RefSeq; YP_892221.1; NC_008599.1.
DR   ProteinModelPortal; A0RPT8; -.
DR   SMR; A0RPT8; 604-797.
DR   STRING; A0RPT8; -.
DR   MEROPS; S16.001; -.
DR   GeneID; 4538035; -.
DR   GenomeReviews; CP000487_GR; CFF8240_1060.
DR   KEGG; cff:CFF8240_1060; -.
DR   NMPDR; fig|360106.5.peg.1013; -.
DR   TIGR; CFF8240_1060; -.
DR   eggNOG; COG0466; -.
DR   OMA; GTILCFY; -.
DR   ProtClustDB; CLSK872549; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008269; Pept_S16_C.
DR   InterPro; IPR004815; Pept_S16_lon.
DR   InterPro; IPR003111; Pept_S16_N.
DR   InterPro; IPR008268; Peptidase_S16_AS.
DR   InterPro; IPR015947; PUA-like_domain.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF02190; LON; 1.
DR   Pfam; PF05362; Lon_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF88697; PUA-like; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   TIGRFAMs; TIGR00763; Lon; 1.
DR   PROSITE; PS01046; LON_SER; 1.
DR   HOGENOMDNA; CAMFF_1.PE1011; -.
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase;
KW   Nucleotide-binding; Protease; Serine protease; Stress response.
SQ   SEQUENCE   798 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQINSIRTFP ANLPVIVEDE LFLYPFMITP LFLNDEKNIK ALDLALRDNT PILVVSSKPQ
     NEGMREFDTC YSAGVIGSVM RRISLPDGRV KILFQGSQKG KIIANISSDP LIALVDTIDI
     ERPSNQKVDA LLSVLREKVK SLSLLNHFFP PDLLKTIDES IEATRVCDLI SSALRLKKGV
     AYDFFIEENL ENRVLKIIDY LIEEIEANKL QKEIKSKVHS KIDKVNKEYF LKEQLKEIQK
     ELGSDVGREE EISEYKNKLE AKKPYMGEDA YKEINKQILK LSRMHPDGSE ASMTGSYLDW
     ALDVPFGNFS KKKLGVKDVA NQLDSDHYGL QKPKKRIVEY FGLRELLELR GLDSKTNNGV
     ILCFAGPPGV GKTSLANSIS KALKRELVRI ALGGLEDVNE LRGHRRTYIG AMPGRIVQGL
     IEAKTMNPVV VLDEIDKLAR SYKGDPTAVL LEVLDPEQNS KFRDYYLNFN VDLSKVIFIA
     TANDIGLIPA PLRDRMEFIS LNSYTPQEKF QIAKKYLIPS ELKKHGLKPS EISITKEALS
     LIIEEYTRES GVRNLRRKIA DILRKVALEI LENKIQKVSI TPKNLKNFLD KKVFEIDSVD
     STDQVGIVNG LAWTSVGGDV LKIEVVRIKG KGSMQITGQL GDVMKESAQI SFSLVKTLID
     TNKIKVPKSM LAKDDKGKEM AVYNSFDLHI HVPEGATPKD GPSAGITMST AIASILSDTP
     IKSDVAMTGE ITLSGKVLPI GGLKEKLIAA YKAKIKTALI PRKNYDRDLE EIPSEVKENM
     QIIPVDTIED VLKLSFSK
//

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