(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBT0_SEGRD

ID   D6ZBT0_SEGRD            Unreviewed;       698 AA.
AC   D6ZBT0;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 52.
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   OrderedLocusNames=Srot_0420 {ECO:0000313|EMBL:ADG96907.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96907.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96907.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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}.
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DR   EMBL; CP001958; ADG96907.1; -; Genomic_DNA.
DR   RefSeq; WP_013137363.1; NC_014168.1.
DR   STRING; 640132.Srot_0420; -.
DR   MEROPS; M41.015; -.
DR   EnsemblBacteria; ADG96907; ADG96907; Srot_0420.
DR   KEGG; srt:Srot_0420; -.
DR   eggNOG; ENOG4105C3H; Bacteria.
DR   eggNOG; COG0465; LUCA.
DR   HOGENOM; HOG000217276; -.
DR   KO; K03798; -.
DR   OMA; MNKRWRN; -.
DR   OrthoDB; 190468at2; -.
DR   BioCyc; SROT640132:G1GLH-421-MONOMER; -.
DR   Proteomes; UP000002247; 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; 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; D6ZBT0.
DR   SWISS-2DPAGE; D6ZBT0.
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:UP000002247};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ADG96907.1};
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   ECO:0000313|EMBL:ADG96907.1};
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:ADG96907.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
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      5     23       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   TRANSMEM    118    140       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   DOMAIN      202    341       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     210    217       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    433    433       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       432    432       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       436    436       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       508    508       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
SQ   SEQUENCE   698 AA;  75151 MW;  1CE2F0DA8E08648E CRC64;
     MNRSALIRIV VIVAAALAIW RIFSYVSDDT RGFQQVDTSV AMKQLDDPAN VESAVLEDSE
     QRLRLKLKHA SSDTGGKTDV YAAIPGGALD KVFEQLEQLR KANGSAAKYN VVNNDPGFLS
     QALVLYGPIL LIGVLFYFAI TRMQNSPRGF GFGRSRAKQL SKDVPKVTFA DVAGADEAVE
     ELYEIKDFLQ NPARYQALGA KIPRGVLLFG PPGTGKTLLA RAVAGEAGVP FFTISGSDFV
     EMFVGVGASR VRDLFEQAKQ ASPCIIFVDE IDAVGRQRGA GFGGGHDERE QTLNQLLVEM
     DGFSERQGVI VMAATNRPDI LDPALLRPGR FDRQIPVGNP DIAGRRAILA VHGKGKPIAP
     DADLEGLAKR TVGMSGADLA NVLNEAALLT ARENGQLITT AALEESVDRV IGGPRRKSRI
     ISELEKKIVA YHESGHTLAG WAMPGLDPVY KVTILARGRT GGHAVTVPED DKGLATRSEL
     IARLVMLLGG RAAEELVFHE PTTGASSDID RATKVARTMV MEYGMSARLG AVRYGDEQED
     PFLGRAMGQR SDYSHEVAKE IDAEVRDLIE AAHTEAWAVL VEYRDQLDAL ATQLLEKETL
     HQKELEEILA GVQKRPKITA FDVFGDRAPS DRPPVKTPRE LAVERGEPWP PVPPHVPAHA
     AGQDQGPAPD APSPSRVPAP ASASLASGPR AAQPHQAG
//

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