(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NRW5_YERPA

ID   A0A0E1NRW5_YERPA        Unreviewed;       644 AA.
AC   A0A0E1NRW5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000256|HAMAP-Rule:MF_01458};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_01458};
DE   Flags: Precursor;
GN   Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN   OrderedLocusNames=YPA_0052 {ECO:0000313|EMBL:ABG12021.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12021.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12021.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12021.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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.
CC       {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_01458}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|RuleBase:RU003651}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR   EMBL; CP000308; ABG12021.1; -; Genomic_DNA.
DR   RefSeq; WP_002228195.1; NZ_CP009906.1.
DR   MEROPS; M41.001; -.
DR   EnsemblBacteria; ABG12021; ABG12021; YPA_0052.
DR   EnsemblBacteria; AJJ79679; AJJ79679; CH58_2888.
DR   KEGG; ypa:YPA_0052; -.
DR   PATRIC; fig|360102.15.peg.3042; -.
DR   KO; K03798; -.
DR   OMA; MNKRWRN; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.58.760; -; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; SSF140990; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1NRW5.
DR   SWISS-2DPAGE; A0A0E1NRW5.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ABG12021.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Metalloprotease {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ABG12021.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   TRANSMEM     98    119       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   NP_BIND     192    199       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    415    415       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       414    414       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       418    418       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       492    492       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
SQ   SEQUENCE   644 AA;  70805 MW;  DDF70E0E9AFF2A43 CRC64;
     MAKNLILWLV IAVVLMSVFQ SFGPSESNGR RVDYSTFMSD VTQDQVREAR INGREINVSK
     KDNSKYTTFI PVNDPKLLDT LLTKNVKVVG EPPEEQSLLA SIFISWFPML LLIGVWIFFM
     RQMQGGGGKG AMSFGKSKAR MLTEDQIKTS FADVAGCDEA KEEVSELVDY LREPSRFQKL
     GGKIPKGVLM VGPPGTGKTL LAKAIAGEAK VPFFTISGSD FVEMFVGVGA SRVRDMFEQA
     KKAAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQMLV EMDGFEGNEG IIVIAATNRP
     DVLDPALLRP GRFDRQVVVG LPDVRGREQI LKVHMRRVPL DTDIDASVIA RGTPGFSGAD
     LANLVNEAAL FAARGNKRVV SMVEFEKAKD KIMMGAERRS MVMTEAQKES TAYHEAGHAI
     IGRLVPEHDP VHKVTIIPRG RALGVTFFLP EGDAISASRQ KLESQISTLY GGRLAEEIIY
     GPEKVSTGAS NDIKVATSIA RNMVTQWGFS EKLGPLLYAE EEGEIFLGRS VAKAKHMSDE
     TARIIDQEVK LLVERNYQRA RKLLLENMDV LHSMKDALMK YETIDAPQID DLMNRKEVRP
     PAGWDNVTKN KSSDNDNTPT ATMPADEPNT PTSGNTVSEQ LGDK
//

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