(data stored in ACNUC7421 zone)

HOGENOM: ACAM1_1_PE2353

ID   ACAM1_1_PE2353                       STANDARD;      PRT;   611 AA.
AC   ACAM1_1_PE2353; B0C453;
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 4; EC=3.4.24 -;
DE   (ACAM1_1.PE2353).
GN   Name=ftsH; Synonyms=ftsH4; OrderedLocusNames=AM1_2436;
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.PE2353.
CC       Acaryochloris marina MBIC11017, complete genome.
CC   -!- ANNOTATIONS ORIGIN:B0C453_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; B0C453; -.
DR   EMBL; CP000828; ABW27444.1; -; Genomic_DNA.
DR   RefSeq; YP_001516758.1; NC_009925.1.
DR   ProteinModelPortal; B0C453; -.
DR   SMR; B0C453; 148-399.
DR   STRING; B0C453; -.
DR   MEROPS; M41.005; -.
DR   GeneID; 5681248; -.
DR   GenomeReviews; CP000828_GR; AM1_2436.
DR   KEGG; amr:AM1_2436; -.
DR   OMA; GGNPAMN; -.
DR   ProtClustDB; CLSK892632; -.
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.PE2353; -.
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   611 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNKRWRNAGL YALLAIVVLA LGTALLERQP ADNPTWRYSK LIEEVENNNV EKIRISADRT
     MAEVKSGEGV ITVNLPPDPD FIDILTKQDV DIAVLPQREE GVWFKALSTF LVPVLLLVGL
     FFLFRRAQSG PGNQAMNFGK SKARVQMEPQ TQVTFNDVAG IEQAKLELTE VVDFLKNADR
     FTAVGAKIPK GVLLVGPPGT GKTLLAKAVA GEAGVPFFSI SGSEFVEMFV GVGASRVRDL
     FEQAKTNAPC IVFIDEIDAV GRQRGAGLGG GNDEREQTLN QLLTEMDGFE GNTGIIIIAA
     TNRPDVLDAA LMRPGRFDRQ VVVDRPDYKG RREILNVHAR GKTLSKDVDL EKMARRTPGF
     TGADLSNLLN EAAILAARRN LTEISMDEIN DAIDRVLAGP EKKDRVMSER RKRLVAYHEA
     GHALVGALMP DYDPVQKISI IPRGRAGGLT WFTPNEDQMD SGLYSRSYLQ NQMAVALGGR
     IAEEIIFGEE EVTTGASNDL QQVARVARQM ITRFGMSDRL GPVALGRQQG NPFMGRDIMS
     ERDFSEETAS TIDDEVRNLV DQAYRRAKDV LVSNRAVLDE IARRLVEKET VDSDELQEIL
     NTNEVKMAAI A
//

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