(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_5_PE233

ID   ACAM1_5_PE233                        STANDARD;      PRT;   655 AA.
AC   ACAM1_5_PE233; A8ZNZ4;
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 -;
DE   (ACAM1_5.PE233).
GN   Name=ftsH; OrderedLocusNames=AM1_D0237;
OS   ACARYOCHLORIS MARINA MBIC11017.
OC   Bacteria; Cyanobacteria; Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACAM1_5.PE233.
CC       Acaryochloris marina MBIC11017 plasmid pREB4, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:FTSH_ACAM1
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 (Potential).
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass
CC       membrane protein; Stromal side (By similarity).
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family.
CC   -!- GENE_FAMILY: HOG000217276 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A8ZNZ4; -.
DR   EMBL; CP000841; ABW32730.1; -; Genomic_DNA.
DR   RefSeq; YP_001522044.1; NC_009929.1.
DR   ProteinModelPortal; A8ZNZ4; -.
DR   SMR; A8ZNZ4; 165-422.
DR   STRING; A8ZNZ4; -.
DR   GeneID; 5686656; -.
DR   GenomeReviews; CP000841_GR; AM1_D0237.
DR   KEGG; amr:AM1_D0237; -.
DR   OMA; WHEIGHA; -.
DR   ProtClustDB; CLSK2393646; -.
DR   BioCyc; AMAR329726:AM1_D0237-MON; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
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; ACAM1_5.PE233; -.
KW   ATP-dependent metalloprotease FtsH-like protein;
KW   ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleotide-binding; Plasmid; Protease; Thylakoid;
KW   Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   655 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPIETEPNRT RKNFEPKRFG GSLFILFTLL LFLNLFVLRG PRFPITAYSD FITQVEAGQV
     ERVEVRPDRI RYILKSDQYG FNEGTETAAV FDTVPVGIDL ELPKFLREHD VQYFAPPPSS
     LSWLPTLLGW VVPPLIFFGI WSWLINRNQG AGPAALTVGQ SKARIYSEGS TGVTFDDVAG
     VEEAKTELLE IVDFLAHADK YTRLGAKIPK GVLLVGPPGT GKTLLAKAIA GEAKVPFFSI
     SGSEFIELFV GIGAARVRDL FEQAKQQAPC IVFIDELDAL GKARGGPGGF TGGNDEREQT
     LNQLLSEMDG FDPNVGVILL AATNRPEVLD PALLRPGRFD RQIVVDRPDK MGREAILKVH
     VRGVKLAEDI NLTKLAVRTP GFSGADLANL VNEAALLAAR QSRDAVVMSD FNEAIERVVA
     GLEKKSRVLN DLEKKTVAYH EVGHAIVGSL MPGAGTVEKI SVIPRGIGAL GYTLQLPEED
     RFLITASELR GRIATLLGGR SAEELIFGVV STGASDDIQK ATDLAERYVT LYGMSDELGP
     IAYEKAQQQF LEGVPNPRRT VGPQVVEAID QAVKDVVDGA HHMALSILSI NQDMLQLTAS
     HLLEKEVLES QELHSLLSQP QFPPDMDEWL QTGKLPQGKE LIQTTLNSHQ LIGIN
//

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