(data stored in ACNUC7421 zone)

SWISSPROT: C6WGG6_ACTMD

ID   C6WGG6_ACTMD            Unreviewed;       743 AA.
AC   C6WGG6;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 58.
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=Amir_0313 {ECO:0000313|EMBL:ACU34282.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34282.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34282.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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}.
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DR   EMBL; CP001630; ACU34282.1; -; Genomic_DNA.
DR   RefSeq; WP_012782945.1; NC_013093.1.
DR   ProteinModelPortal; C6WGG6; -.
DR   STRING; 446462.Amir_0313; -.
DR   MEROPS; M41.015; -.
DR   EnsemblBacteria; ACU34282; ACU34282; Amir_0313.
DR   KEGG; ami:Amir_0313; -.
DR   eggNOG; ENOG4105C3H; Bacteria.
DR   eggNOG; COG0465; LUCA.
DR   HOGENOM; HOG000217276; -.
DR   KO; K03798; -.
DR   OMA; MNKRWRN; -.
DR   OrthoDB; POG091H02HH; -.
DR   Proteomes; UP000002213; 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-HAMAP.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
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   Pfam; PF00004; AAA; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGG6.
DR   SWISS-2DPAGE; C6WGG6.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000313|EMBL:ACU34282.1};
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:ACU34282.1};
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:ACU34282.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213};
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     12     28       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   TRANSMEM    117    135       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   DOMAIN      198    337       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     206    213       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    429    429       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       428    428       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       432    432       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       504    504       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
SQ   SEQUENCE   743 AA;  80925 MW;  C41250C104C7A6C0 CRC64;
     MDRKRLLRNP LLWIVAVVLL FYVFSVLFDE DRNYHQVTTS QALQQVRDGK VKEATIEDKE
     QKLKLVLNDG STFENHGLLM ASYPASATDE VFTLVDQAGN KPQVETKVTQ DSLLTQMLLY
     LVPLGLLLLL LMWMMNNAQG GGNRVLNFGK SKAKQLSKDM PKTTFADVAG AEEAVEELYE
     IKDFLQNPGR YQALGAKIPK GVLLYGPPGT GKTLLARAVA GEAGVPFYSI SGSDFVEMFV
     GVGASRVRDL FEQAKQNAPC IIFVDEIDAV GRHRGAGMGG GHDEREQTLN QLLVEMDGFD
     SRGGIILIAA TNRPDILDPA LLRPGRFDRQ IPVSAPDLKG RKQILRVHAK GKPLAPDTDL
     DGLAKRTVGF SGADLANVIN EAALLTARQN GTVIDGSALE ESVDRVIGGP ARKSRIISEK
     EKKITAYHEA GHALAAWAMP DIDPVYKVTI LARGRTGGHT LSVPEEDKDL MTRSEMIARL
     VFALGGRSAE ELVFHEPTTG ASNDIEQATK IARAMVTEYG MSSRLGAVKY GQEQGEPFLG
     RNAGRQADYS LEVAHEIDEE VRKLIEAAHT EAYEVLNTYR DVLDDLTLEL IDKETLHQKD
     LERIFAGVEK RPRITQFNDF GNRIPSTKPP VKTPGELARE RGEPWPPVVE DQVEAEPAAL
     PAPAPETPQG PAQPQQVPAG ANGVQHPPQQ VTPGSGPPNY GAPPGWTPAT VPGSGGQPTT
     PAWRPDPADA DKRNFDSDPD NRK
//

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