(data stored in ACNUC7421 zone)

HOGENOM: ACCPU_4_PE3622

ID   ACCPU_4_PE3622                       STANDARD;      PRT;   624 AA.
AC   ACCPU_4_PE3622; C7RKS7;
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   RecName: Full=ATP-dependent zinc metalloprotease FtsH; EC=3.4.24 -;Flags:
DE   Precursor; (ACCPU_4.PE3622).
GN   Name=ftsH; OrderedLocusNames=CAP2UW1_3747;
OS   CANDIDATUS ACCUMULIBACTER PHOSPHATIS CLADE IIA STR. UW-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=522306;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACCPU_4.PE3622.
CC       Candidatus Accumulibacter phosphatis clade IIA str. UW-1, complete geno
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C7RKS7_ACCPU
CC   -!- FUNCTION: Acts as a processive, ATP-dependent zinc
CC       metallopeptidase for both cytoplasmic and membrane proteins. Plays
CC       a role in the quality control of integral membrane proteins (By
CC       similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homohexamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family.
CC   -!- GENE_FAMILY: HOG000217276 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C7RKS7; -.
DR   EMBL; CP001715; ACV36997.1; -; Genomic_DNA.
DR   RefSeq; YP_003168926.1; NC_013194.1.
DR   ProteinModelPortal; C7RKS7; -.
DR   STRING; C7RKS7; -.
DR   GeneID; 8405916; -.
DR   GenomeReviews; CP001715_GR; CAP2UW1_3747.
DR   KEGG; app:CAP2UW1_3747; -.
DR   ProtClustDB; CLSK2525772; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:HAMAP.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:HAMAP.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   HAMAP; MF_01458; FtsH; 1; -.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; Pept_M41_FtsH.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
DR   HOGENOMDNA; ACCPU_4.PE3622; -.
KW   ATP-dependent metalloprotease FtsH;
KW   ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Nucleotide-binding; Protease; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
SQ   SEQUENCE   624 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MFKNLAIWLV IGLVLMTVFN QFNTRQVAQS SMEYSQFIEE VGKGTIAKVV IEGRVLKATT
     TDGRKLTSYA PPDLWMVSDL LKHGVKIEAK PEEEQSFLMS IFVSWFPMLL LIGVWVFFMR
     QMQGGGRGGA FSFGKSKARL LDESTNTITF ADVAGCDEAK EEVSELVDFL RDPSKFQKLG
     GRIPKGVLLV GNPGTGKTLL AKAIAGEAKV PFFSISGSDF VEMFVGVGAA RVRDMFENAK
     KHAPCIIFID ELDAVGRQRG AGLGGGNDER EQTLNQMLVE MDGFEGSVGV IVIAATNRPD
     VLDPALMRPG RFDRQVVVPL PDIRGREQIL VVHMRKVPLS PDVKADIIAR GTPGFSGADL
     ANLVNEAALF AARGNKRLVD MEDFEKAKDK IMMGAERRSM VMNEDERRNT AYHESGHAVV
     AKLMPKSDPV HKVTIIPRGR ALGLTMQLPE EDRYAYDRVY LMSRIAVLFG GRIAEELFMN
     QMTTGASNDF ERATQMARDM VTRYGMSDAL GPMVYGENEG EVFLGRSVTT HKNMSEATME
     KVDAEIRRII DEQYALARRL LEENRSRVEA MATALLELET IDSDQIDDIM AGKPPRPPKQ
     PQSRSSSRPD NNAPDAAPSA TAPA
//

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