(data stored in ACNUC1104 zone)

SWISSPROT: A4F6S0_SACEN

ID   A4F6S0_SACEN            Unreviewed;       795 AA.
AC   A4F6S0;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 85.
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};
GN   Name=ftsH {ECO:0000256|HAMAP-Rule:MF_01458,
GN   ECO:0000313|EMBL:CAL99744.1};
GN   OrderedLocusNames=SACE_0396 {ECO:0000313|EMBL:CAL99744.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99744.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99744.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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 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; AM420293; CAL99744.1; -; Genomic_DNA.
DR   RefSeq; WP_009946439.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0396; -.
DR   MEROPS; M41.015; -.
DR   EnsemblBacteria; CAL99744; CAL99744; SACE_0396.
DR   KEGG; sen:SACE_0396; -.
DR   eggNOG; ENOG4105C3H; Bacteria.
DR   eggNOG; COG0465; LUCA.
DR   HOGENOM; HOG000217276; -.
DR   KO; K03798; -.
DR   OMA; MNKRWRN; -.
DR   OrthoDB; 190468at2; -.
DR   BioCyc; SERY405948:SACE_RS01945-MONOMER; -.
DR   Proteomes; UP000006728; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 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; A4F6S0.
DR   SWISS-2DPAGE; A4F6S0.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Cell cycle {ECO:0000313|EMBL:CAL99744.1};
KW   Cell division {ECO:0000313|EMBL:CAL99744.1};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:CAL99744.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000006728};
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   DOMAIN      183    322       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     191    198       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    414    414       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       413    413       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       417    417       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       489    489       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
SQ   SEQUENCE   795 AA;  85765 MW;  A6DC43DB872B83F8 CRC64;
     MTAFLLIYAF SVLFDETRNY REVSTSQALE QIAQGKVKEA TIEDKEQRVR LTLKDGQTFE
     NSSELIAQYP AGATDQVVQE IRNGQVPSWN TKVTQDSFWV QMLFYLVPIG LLVLLLMWMM
     NNVQGGGNRV LNFGKSKAKQ LTKDMPKTLF GDVAGADEAV EELHEIKDFL QNPGRYQALG
     AKIPKGVLLY GPPGTGKTLL ARAVAGEAGV PFYSISGSDF VEMFVGVGAS RVRDLFEQAK
     QNAPCIVFVD EIDAVGRQRG AGLGGGHDER EQTLNQLLVE MDGFDSRGGI ILIAATNRPD
     ILDPALLRPG RFDRQIPVSA PDLRGRRAIL GVHSKGKPLA QDADLDGLAK RTVGFSGADL
     ENVVNEAALL TARENGQLIT AAALEESVDR VIGGPRRKSK IISERDKKIT AYHEGGHALA
     AWAMPDLEPV YKLTILPRGR TGGHALVVPE DDKDMMTRSE MIARLVFALG GRSAEELVFH
     EPTTGASSDI EQATKIARAM VTEYGMTARL GAVKYGKEEG DPFLGRSAGQ QPNYSLEVAH
     EIDEEVRKLI EAAHTEAWEI LNTYRDVLDE LVLELIEKET LVRKDLERIF TKVEKRPRIT
     AFNDFGGRTP SEKPPIKTPG ELARERGEPW PPVTEQPPAP APTPVGAGQQ QGDASQSNGV
     GQYGQHPGTV QFPNPGHQQG QQGGYQQPGQ GQYGQPVPQA VPPNYGAPPG WTPATSPSGS
     APSGAPVPSG AEQGGNQYNW VPSWERSQQP QTGPSQPGGG DSNGTPGAQP AQGEGQSGQS
     PDSTDENGNG TSTNR
//

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