(data stored in ACNUC7421 zone)

HOGENOM: ACHLI_1_PE1333

ID   ACHLI_1_PE1333                       STANDARD;      PRT;   641 AA.
AC   ACHLI_1_PE1333; A9NE17;
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   (ACHLI_1.PE1333).
GN   Name=ftsH; OrderedLocusNames=ACL_1386;
OS   ACHOLEPLASMA LAIDLAWII PG-8A.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC   Acholeplasma.
OX   NCBI_TaxID=441768;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACHLI_1.PE1333.
CC       Acholeplasma laidlawii PG-8A chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:FTSH_ACHLI
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: Cell membrane; Multi-pass membrane protein;
CC       Cytoplasmic 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; A9NE17; -.
DR   EMBL; CP000896; ABX81977.1; -; Genomic_DNA.
DR   RefSeq; YP_001621353.1; NC_010163.1.
DR   ProteinModelPortal; A9NE17; -.
DR   SMR; A9NE17; 178-425.
DR   STRING; A9NE17; -.
DR   GeneID; 5803761; -.
DR   GenomeReviews; CP000896_GR; ACL_1386.
DR   KEGG; acl:ACL_1386; -.
DR   OMA; CEEMFAI; -.
DR   BioCyc; ALAI441768:ACL_1386-MON; -.
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:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion 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: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; 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; ACHLI_1.PE1333; -.
KW   mebrane-bound ATP-dependent metalloprotease;
KW   ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW   Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   641 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNKQQKPKRS PLRPDYLVIV IIILLAIGMY FFFTEMMAPK VKQFDEFEFI AAIESGQIAT
     VRSEYVGGDN FNLWEVTGTF TTGNAPEGVG SYVIILYGDR LNNIQDIIIT YNELNPSTPI
     TVSFVPHVSV DFWNIISTLL LIAAPIVLVV IMFRSMSSQS NKAQDFTKNR AKLSQGRKVK
     FSDIAGADEE KAEMAELIDF LKNPKKYADM GARVPKGVLL VGQPGTGKTL LAKAVAGEAQ
     VPFFSISGSD FVELYVGVGA SRVRDLFKVA KQSAPCIIFI DEIDAVGRQR GAGMGGGNDE
     REQTLNQLLV EMDGFSANLG IIIMAATNRP DVLDPALLRP GRFDRQITMQ VPDQKSREEI
     LKVHARSKKL DPTIKFSEVA MRIPGFTGAD IENLLNEAAL LAARESRTVI SMQDIDEAAD
     RVTMGPAKKS RKYSPNEKKM VAYHEAGHAV IGLKVNLAST VQKVTIVPRG RAGGYALYTP
     VEEKFNYAKS ELLAMITSAL GGRVAEEIMF DDVTTGAYDD FKRATKLARS MVTEYGMSDL
     GPIQYESDSG NVFLGRDYLK DKNFSDAVAL EIDREVRAII TECYEHARKV INENKNLLDN
     IAKYLIAVET LTKTDIDEIA ATGQLQWWDN REVEEDSKKS E
//

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