FTSH_PARUW
ID FTSH_PARUW Reviewed; 916 AA.
AC Q6MDI5;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH;
DE EC=3.4.24.-;
GN Name=ftsH; OrderedLocusNames=pc0640;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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 (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homohexamer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000305}.
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DR EMBL; BX908798; CAF23364.1; -; Genomic_DNA.
DR RefSeq; WP_011175190.1; NC_005861.1.
DR AlphaFoldDB; Q6MDI5; -.
DR SMR; Q6MDI5; -.
DR STRING; 264201.pc0640; -.
DR EnsemblBacteria; CAF23364; CAF23364; PC_RS03065.
DR KEGG; pcu:PC_RS03065; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_7_2_0; -.
DR OMA; RQMKGMG; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000000529; 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:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..916
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400379"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..371
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..916
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..92
FT /note="Unknown"
FT REGION 93..916
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT REGION 883..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 687
FT /evidence="ECO:0000250"
FT BINDING 464..471
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 686
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 762
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 916 AA; 102325 MW; 2C5CBD59F38236D9 CRC64;
MSDDNKQDFK KGISNSFVWF LMAAFLFALM VQNFIDTKFA KVSFSYQLEH LVNLQLLQPE
DSRKIALNDN LVTFSGKFRD RLTEEGKTRY KYLELLDTNH ELKAEQARVK DEIKTLKTKV
FDSASLFLQL SGLSIPKGGY VVVDDMYNTP EEDQSVVIKD LPKSAVESLV SLEKEYEAAR
QNPTAESLKN LGNLINELLR NLRSPALGIG SETIKQSLKG IDKEVADSGA TSLSEQLAAY
GHALVNLKAI IDELNHEEDH IRLAKLRSVR NYKETLDEYN QINTRLDDNQ IQLDKARQSV
SNVIWYFNNQ ELSTKALEKQ DPEVYNQWFS KAKEEWANFS HNRGGIFRAP DQPLNAVLEK
TFKSEEPSPN YFSYLFTLLP VLLVILVLYM LFARQMKGMG NTAMNFGKSP ARLLNKGDNK
ITFKDVAGVD EALEELQEIV EFLKNPQKFT SLGGKIPKGV LCIGPPGTGK TLIAKAVAGE
ADRPFFSISG SDFVEMFVGV GASRIRDLFE QAKKAAPCII FMDEIDAVGR HRGVGMGGGH
DEREQTLNQL LVEMDGFDTN EGVILMAATN RPDVLDKALL RPGRFDRRVI IGLPDIKGRY
DILKVHARRI KMDPSIDLMA IARSTPGSSG ADLANILNES ALLAARKGRT AVTAQETIEA
RDKVLYGKER RSLEIDENEK RTTAYHESGH TVVGLIVKSG DPVDKVTIIP RGMSLGATMF
LPKKNRVSYW KQELHDQLAV LMGGRVAEEI FVGDVSSGAQ QDIERATQLA RSMVCKWGMS
DKLGAVAYDE RSEGGGQYGF GDHHEKTYSD ETAQAIDSEV RRILDEALAI ARKIILDYKE
QVELLTLMLI EFETLDSEDI QEIVVKNNWD AVRKRERLKR AADLHKKEAA TPPPPPPREV
DISSSGTIPN TLGLSS
