ID A0A3R9PXS1_9BACI Unreviewed; 698 AA.
AC A0A3R9PXS1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 ORFNames=D7Z54_31820 {ECO:0000313|EMBL:RSL29316.1};
OS Salibacterium salarium.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=284579 {ECO:0000313|EMBL:RSL29316.1, ECO:0000313|Proteomes:UP000275076};
RN [1] {ECO:0000313|EMBL:RSL29316.1, ECO:0000313|Proteomes:UP000275076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IM0101 {ECO:0000313|EMBL:RSL29316.1,
RC ECO:0000313|Proteomes:UP000275076};
RA Yamprayoonswat W., Boonvisut S., Jumpathong W., Sittihan S., Ruangsuj P.,
RA Wanthongcharoen S., Thongpramul N., Pimmason S., Yu B., Yasawong M.;
RT "Draft genome sequence of Bacillus salarius IM0101, isolated from a
RT hypersaline soil in Inner Mongolia, China.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000256|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01458};
CC 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSL29316.1}.
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DR EMBL; RBVX01000075; RSL29316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R9PXS1; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000275076; Unassembled WGS sequence.
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; 3.40.50.300; 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 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:UP000275076};
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 9..26
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 199..338
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 609..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 433
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 505
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 698 AA; 76866 MW; 911FA0C8D35C5736 CRC64;
MNRIFRNTVF YLLLFLVIIG IISFLSNDQT DTSELSTEEF MTKLENDEIA SVTLQPEGEV
YLVEGKEVGQ GEDESFQTYM PISEENTQML MTAAQGANGE ALDLDTKPAE EPSAWVTFFT
SIIPFVIIFI LFFFLLSQAQ GGGSKMMNFG KSKAKLYQEE KKKERFKDVA GAEEEKQELV
EVVDFLKDPR KFASIGARIP KGVLLVGPPG TGKTLIARAV AGEAGVPFFS ISGSDFVEMF
VGVGASRVRD LFENAKKNAP CIIFIDEIDA VGRQRGAGVG GGHDEREQTL NQLLVEMDGF
SANEGIIIIA ATNRSDVLDP ALLRPGRFDR QIMVGRPDVK GREEVLGVHA RNKPLADDVN
LKAIAQRTPG FTGADLENLL NEAALVAARS DMEKIRMSHI EEAIDRVIAG PAKKSRVISE
KEKNIVAHHE AGHTVVGVKL ENADMVHKVT IVPRGQAGGY AVMLPKEDRF FMTKPELIDK
IVGLLGGRVA EEVMFNEVST GAHNDFQRTT DIARKMVTEY GMSDKLGPIQ FGSSGGGQVF
LGRDIQNEQN YSDAIAHEID KEVQNIVNEC YERCKQILTE NKDKLEAVAA ALLELETLDA
EQIESLVEKG ELPEDHHLNK EDDEVGVTNK PDHSDNEGQD GDVKVNIQSK SDSDEEQTEA
SRAEDDKRTK NDNVENKSEA EKLGSNNPPS SEDDEDRK
//
