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FTSH_STRR6
ID   FTSH_STRR6              Reviewed;         652 AA.
AC   P59652;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE            EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN   Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=spr0012;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
CC   -!- FUNCTION: Acts as a processive, ATP-dependent zinc metallopeptidase for
CC       both cytoplasmic and membrane proteins. Plays a role in the quality
CC       control of integral membrane proteins. {ECO:0000255|HAMAP-
CC       Rule:MF_01458}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01458};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01458};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01458}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR   EMBL; AE007317; AAK98816.1; -; Genomic_DNA.
DR   RefSeq; NP_357606.1; NC_003098.1.
DR   RefSeq; WP_000744557.1; NC_003098.1.
DR   AlphaFoldDB; P59652; -.
DR   SMR; P59652; -.
DR   STRING; 171101.spr0012; -.
DR   MEROPS; M41.009; -.
DR   EnsemblBacteria; AAK98816; AAK98816; spr0012.
DR   GeneID; 60232786; -.
DR   KEGG; spr:spr0012; -.
DR   PATRIC; fig|171101.6.peg.13; -.
DR   eggNOG; COG0465; Bacteria.
DR   HOGENOM; CLU_000688_16_2_9; -.
DR   OMA; QYGMTER; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   Gene3D; 1.20.58.760; -; 1.
DR   Gene3D; 3.40.50.300; -; 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;
KW   ATP-binding; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..652
FT                   /note="ATP-dependent zinc metalloprotease FtsH"
FT                   /id="PRO_0000084651"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        33..131
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   TOPO_DOM        153..652
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   REGION          628..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        450
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         227..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         449
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         453
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT   BINDING         525
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   652 AA;  71254 MW;  9055E4363400E45E CRC64;
     MKKQNNGLIK NPFLWLLFIF FLVTGFQYFY SGNNSGGSQQ INYTELVQEI TDGNVKELTY
     QPNGSVIEVS GVYKNPKTSK EGTGIQFFTP SVTKVEKFTS TILPADTTVS ELQKLATDHK
     AEVTVKHESS SGIWINLLVS IVPFGILFFF LFSMMGNMGG GNGRNPMSFG RSKAKAANKE
     DIKVRFSDVA GAEEEKQELV EVVEFLKDPK RFTKLGARIP AGVLLEGPPG TGKTLLAKAV
     AGEAGVPFFS ISGSDFVEMF VGVGASRVRS LFEDAKKAAP AIIFIDEIDA VGRQRGVGLG
     GGNDEREQTL NQLLIEMDGF EGNEGIIVIA ATNRSDVLDP ALLRPGRFDR KVLVGRPDVK
     GREAILKVHA KNKPLAEDVD LKLVAQQTPG FVGADLENVL NEAALVAARR NKSIIDASDI
     DEAEDRVIAG PSKKDKTVSQ KERELVAYHE AGHTIVGLVL SNARVVHKVT IVPRGRAGGY
     MIALPKEDQM LLSKEDMKEQ LAGLMGGRVA EEIIFNVQTT GASNDFEQAT QMARAMVTEY
     GMSEKLGPVQ YEGNHAMLGA QSPQKSISEQ TAYEIDEEVR SLLNEARNKA AEIIQSNRET
     HKLIAEALLK YETLDSTQIK ALYETGKMPE AVEEESHALS YDEVKSKMND EK
 
 
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