(data stored in ACNUC7421 zone)

HOGENOM: ACIB5_2_PE3002

ID   ACIB5_2_PE3002                       STANDARD;      PRT;   598 AA.
AC   ACIB5_2_PE3002; B7I635;
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   (ACIB5_2.PE3002).
GN   Name=ftsH; OrderedLocusNames=AB57_3096;
OS   ACINETOBACTER BAUMANNII AB0057.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter; Acinetobacter calcoaceticus/baumannii
OC   complex.
OX   NCBI_TaxID=480119;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIB5_2.PE3002.
CC       Acinetobacter baumannii AB0057, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:B7I635_ACIB5
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: Cell inner membrane; Multi-pass membrane
CC       protein; Cytoplasmic 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; B7I635; -.
DR   EMBL; CP001182; ACJ41681.1; -; Genomic_DNA.
DR   RefSeq; YP_002320417.1; NC_011586.1.
DR   ProteinModelPortal; B7I635; -.
DR   SMR; B7I635; 113-367.
DR   STRING; B7I635; -.
DR   GeneID; 7045138; -.
DR   GenomeReviews; CP001182_GR; AB57_3096.
DR   KEGG; abn:AB57_3096; -.
DR   OMA; KKESTNI; -.
DR   ProtClustDB; CLSK830697; -.
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: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:0051301; P:cell division; IEA:UniProtKB-KW.
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; ACIB5_2.PE3002; -.
KW   cell division protein FtsH;
KW   ATP-binding; Cell division; Cell inner membrane; Cell membrane;
KW   Complete proteome; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleotide-binding; Protease; Transmembrane;
KW   Transmembrane helix; Zinc.
SQ   SEQUENCE   598 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKYSDFVAAV NAGQIKQVTI DGLNISGEKT NGSQFETVRP QVEDTELMPS LNKQNVVVEG
     TAPQRQGILM QLLIASFPVL LIILLFMFFM RNMGGGAGGK NGPMSFGKSK AKMLSEDQIK
     VTFADVAGCD EAKQEVVEIV DFLKDPAKFK RLGATIPRGV LMVGPPGTGK TLLAKAIAGE
     AKVPFFSISG SDFVEMFVGV GASRVRDMFE QAKRHAPCII FIDEIDAVGR HRGSGTGGGH
     DEREQTLNQM LVEMDGFEGN EGVIVIAATN RVDVLDKALL RPGRFDRQVM VGLPDIRGRE
     QILNVHLKKL PSVTGVDVKV LSRGTPGFSG AQLANLVNEA ALFAARRNKN TVDMHDFEDA
     KDKIYMGPER KSMVLREEER RATAYHEAGH AIVAEILPGT DPVHKVTIMP RGWALGVTWQ
     LPEQDQISHY KDKMLNEIAI LFGGRIAEEV FIQQQSTGAS NDFERATKMA RAMVTKYGMS
     DKMGVMVYED ENQNGFFGNV GSRTISEATQ QQVDQEVRRI LDEQYKVARD ILENNKDIAH
     AMVKALMEWE TIDRDQIRDI MEGREPQPPK VYIAENPVSA FEPPKDGPST PPPLPAMN
//

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