FTSH_CHLT2
ID FTSH_CHLT2 Reviewed; 913 AA.
AC B0B970;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH;
DE EC=3.4.24.-;
GN Name=ftsH; OrderedLocusNames=CTL0213;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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; AM884176; CAP03657.1; -; Genomic_DNA.
DR RefSeq; WP_009873450.1; NC_010287.1.
DR RefSeq; YP_001654303.1; NC_010287.1.
DR AlphaFoldDB; B0B970; -.
DR SMR; B0B970; -.
DR EnsemblBacteria; CAP03657; CAP03657; CTL0213.
DR KEGG; ctb:CTL0213; -.
DR PATRIC; fig|471472.4.peg.230; -.
DR HOGENOM; CLU_000688_7_1_0; -.
DR OMA; RQMKGMG; -.
DR Proteomes; UP000000795; 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 Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..913
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_5000301031"
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..373
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..913
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..100
FT /note="Unknown"
FT REGION 101..913
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT REGION 887..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 689
FT /evidence="ECO:0000250"
FT BINDING 466..473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 688
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 913 AA; 101815 MW; 30C72E71A6A0EF9C CRC64;
MAKDKKTNPE SKKSFPTAFF FLLFGVIFGV VTVQNFFSAK KASVGFSHQL EHLVNLKLLI
PEESRKTALN DNLVSFSGRF REVVPAEGQV RYQYLDLIER KHQIDFELEE ASKSLTVLSK
EVRNAITWFS AISGMPIPEA GYTISPRTDV GLSVLEPLVV YGPVDAQIVN LAALENRVRS
LPKSTESLRV FGSDLYALIG KYLSPALGIG SESLKKEIKD LHQQVENSLT QVIEGDQAVA
LYKTVLETLH RISLALVSPE EGTRFHQLRS VRLYREDFNR CVKLLRESDE TQVQLDKLRG
ELVQAVWYFN NQELSSRALE KQDPEVFSRW FEGAKQEWAA FSSNKSLSFR APDQPRNLVL
EKTFRSEEPT PHYSGYLFTF MPIILVLLFI YFIFSRQVKG MNGSAMSFGK SPARLLAKGQ
NKVTFADVAG IEEAKEELVE IVDFLKNPTK FTSLGGRIPK GILLIGAPGT GKTLIAKAVA
GEADRPFFSI AGSDFVEMFV GVGASRIRDM FEQAKRNAPC IIFIDEIDAV GRHRGAGIGG
GHDEREQTLN QLLVEMDGFG TNEGVILMAA TNRPDVLDKA LLRPGRFDRR VVVNLPDIKG
RFEILAVHAK RIKLDPTVDL MAVARSTPGA SGADLENLLN EAALLAARKD RTAVTAVEVA
EARDKVLYGK ERRSLEMDAQ EKKTTAYHES GHAIVGLCVE HSDPVDKVTI IPRGLSLGAT
HFLPEKNKLS YWKKELYDQL AVLMGGRAAE QIFLGDVSSG AQQDIAQATK IVRSMICEWG
MSDHLGTVAY DEHSEAAPTG YGSYHEKNYS EETAKVIDNE LKTLLDAAYQ RALDIINSHK
EELELMTQML IEFETLDSKD VKEIMDHSWD ADKKRARMKE EGMLYKKISE DLPPPPPQEN
VQDGTSLKFN TST
