(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE4477

ID   ACAM1_1_PE4477                       STANDARD;      PRT;   631 AA.
AC   ACAM1_1_PE4477; B0BZC0;
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 7; EC=3.4.24 -;
DE   (ACAM1_1.PE4477).
GN   Name=ftsH; Synonyms=ftsH7; OrderedLocusNames=AM1_4590;
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_1.PE4477.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:B0BZC0_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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass
CC       membrane protein; Stromal 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; B0BZC0; -.
DR   EMBL; CP000828; ABW29564.1; -; Genomic_DNA.
DR   RefSeq; YP_001518882.1; NC_009925.1.
DR   ProteinModelPortal; B0BZC0; -.
DR   SMR; B0BZC0; 163-417.
DR   STRING; B0BZC0; -.
DR   GeneID; 5683392; -.
DR   GenomeReviews; CP000828_GR; AM1_4590.
DR   KEGG; amr:AM1_4590; -.
DR   OMA; LWMFVFR; -.
DR   ProtClustDB; CLSK2401736; -.
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: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; ACAM1_1.PE4477; -.
KW   ATP-dependent metalloprotease FtsH-like protein;
KW   ATP-binding; Complete proteome; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleotide-binding; Protease; Thylakoid;
KW   Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   631 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPIKDKPQRP RPNVVTSLLL FLPAILLIAN LALPFVMGPR VPRVPYSFFI EQVRDEQVAR
     VSVGQKLIRY QLKDDTAEES KILETTPIFD LELPKLLESK GVEFAATPPP SNRWFTTLLS
     WVIPPVIFVA IFQFFSRGGI GGGGPQGALS VTKNKAKVYV EGDDNKVTFD DVAGVEESKT
     ELEEIVEFLK SPQRFTEIGA KIPKGVLLVG PPGTGKTLMA KAVAGEAGVP FFSISGSEFV
     ELFVGTGAAR VRDLFEQAKK KAPCIIFIDE LDAIGKSRAG GNGFVGGNDE REQTLNQLLT
     EMDGFGAGDA TVIVLAATNR PETLDPALLR PGRFDRQVLV DRPDLSGRLA ILEIYAKKVK
     LGDNVDLKAM ATRTPGFAGA DLANLVNEAA LLAARRDSKV VETQDFAEAI ERVVAGLEKK
     SRVLNDKEKK IVAYHEVGHA LVGAKMSGTD QVEKISIVPR GMAALGYTLQ VPTEDRFLLN
     ESELKGQIAT LLGGRAAEEV IFGSITTGAS NDLQRATDLA EQMVTSYGMS EVLGPLAYDK
     GQQNNFLGGG MNARRMVSDE TAKAIDKEVK GIVETAHQEA LSILKENKEL LETISEQLLE
     SEVIEGEGLR QMLAKVHPES HVQATEEPVT L
//

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