ID A1WXX2_HALHL Unreviewed; 651 AA.
AC A1WXX2;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=Hhal_1770 {ECO:0000313|EMBL:ABM62534.1};
OS Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS halophila (strain DSM 244 / SL1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM62534.1, ECO:0000313|Proteomes:UP000000647};
RN [1] {ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA Richardson P.;
RT "Complete sequence of Halorhodospira halophila SL1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABM62534.1, ECO:0000313|Proteomes:UP000000647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX PubMed=23991253; DOI=10.4056/sigs.3677284;
RA Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT "Complete genome sequence of Halorhodospira halophila SL1.";
RL Stand. Genomic Sci. 8:206-214(2013).
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:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-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-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 M41
CC family. {ECO:0000256|ARBA:ARBA00010044, ECO:0000256|HAMAP-
CC Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000256|HAMAP-Rule:MF_01458}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
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DR EMBL; CP000544; ABM62534.1; -; Genomic_DNA.
DR RefSeq; WP_011814556.1; NC_008789.1.
DR AlphaFoldDB; A1WXX2; -.
DR STRING; 349124.Hhal_1770; -.
DR MEROPS; M41.001; -.
DR KEGG; hha:Hhal_1770; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_0_6; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000000647; Chromosome.
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 CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 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 NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01458};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01458};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01458};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
KW Reference proteome {ECO:0000313|Proteomes:UP000000647};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01458}; Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 190..329
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 595..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 421
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 651 AA; 71783 MW; B52561195E479562 CRC64;
MSDMAKNLIL WVIIAVVLMS VFSNFQEQSA DVTEKVPYSE FLNEVERGNI REVLIRGEEI
TIQHADGNEY RTFNPEVDNR ALIGELLEHG VTIDAEQAES DSMLMQILIS WTPFLLLIAV
WIYFMRQMQG GGGGRGAMSF GKSKAKMMTE EQSKHSFSDV AGCDEAKEDV KELVDFLRDP
SKFQKLGGTI PRGVLMVGPP GTGKTLLAKA IAGEARVPFF SISGSDFVEM FVGVGASRVR
DMFQQAKKQA PCIIFIDELD AVGRQRGAGL GGGHDEREQT LNQMLVEMDG FEGSEGIIVI
AATNRPDVLD PALLRPGRFD RQVVVPLPDV RGREQILNVH MRKVPTADDV RPEIIARGTP
GFSGADLQNL VNEAALFAAR ANKEAVDQTD FEQAKDKIMM GSERKSMVMK EDEKKLTAYH
EAGHAIVGLL TPEHDPVHKV TIIPRGRALG VTMFLPEEDR YSYTKQRLDS MIASLFGGRI
AEELIFGNDR VTTGAQNDIQ RATEIARNMV TKWGLSARLG PLAYGEEEGE VFLGRSMAQQ
KDVSDETQHA IDEEVRAVID NNYTAAEKIL QENLEKLHLM ADALMKYETI DRDQIDDIMR
GDEPRPPKGW QDRDHGGGSG DEGETAGADD QPEAEGKDGR EGPIGGPVGE H
//
