(data stored in ACNUC30567 zone)

HOGENOM: ACAM1_1_PE1532

ID   ACAM1_1_PE1532                       STANDARD;      PRT;   635 AA.
AC   ACAM1_1_PE1532; B0CA36;
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 2; EC=3.4.24 -;
DE   (ACAM1_1.PE1532).
GN   Name=ftsH; Synonyms=ftsH2; OrderedLocusNames=AM1_1599;
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.PE1532.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:B0CA36_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; B0CA36; -.
DR   EMBL; CP000828; ABW26623.1; -; Genomic_DNA.
DR   RefSeq; YP_001515937.1; NC_009925.1.
DR   ProteinModelPortal; B0CA36; -.
DR   SMR; B0CA36; 161-415.
DR   STRING; B0CA36; -.
DR   GeneID; 5680418; -.
DR   GenomeReviews; CP000828_GR; AM1_1599.
DR   KEGG; amr:AM1_1599; -.
DR   OMA; RRINDKE; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; 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; IPR000642; Peptidase_M41.
DR   Pfam; PF00004; AAA; 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.PE1532; -.
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   635 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPVNDKPRRP NPFRTILLLL PLGLLVLNLV LTFGNGPRVS KVPYSFFLEQ VQDGEVARVS
     VGQDIIRYQL KGMEGNAGQV QETTPIFDLE LPKLLEANDV EFAATPPAGN RWFTTLLSWV
     IPPVIFVAIF QFFSRGGIGG GGPQGALSVT KNKAKVYVEG DDNKVTFDDV AGVEESKTEL
     EEIVEFLKSP QRFTEIGAKI PKGVLLVGPP GTGKTLMAKA VAGEAGVPFF SISGSEFVEL
     FVGTGAARVR DLFEQAKKKA PCIIFIDELD AIGKSRAGGN GFVGGNDERE QTLNQLLTEM
     DGFGAGDATV IVLAATNRPE TLDPALLRPG RFDRQVLVDR PDLTGRLAIL EIYAKKVKLG
     ENVDLKAMAT RTPGFAGADL ANLVNEAALL AARRGSKVVE TQDFAEAIER VVAGLEKKSR
     VLNEKEKKIV AYHEVGHALV GAKMSGTDQV EKISIVPRGM AALGYTLQVP TEDRFLLNES
     ELKGQIATLL GGRAAEEVIF GSITTGASND LQRATDLAEQ MVTSYGMSEV LGPLAYDKGQ
     QNNFLGGGMN ARRAVSDETA KEIDKEVKGI VETAHQEALS ILKENKELLE TISEQLLEKE
     VIEGNGLREM LAKVHPELEG QTEQHVQETE KPLAV
//

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