ID A0A1T5DNK8_9SPHI Unreviewed; 696 AA.
AC A0A1T5DNK8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=SAMN05661099_2470 {ECO:0000313|EMBL:SKB73239.1};
OS Daejeonella lutea.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Daejeonella.
OX NCBI_TaxID=572036 {ECO:0000313|EMBL:SKB73239.1, ECO:0000313|Proteomes:UP000189981};
RN [1] {ECO:0000313|Proteomes:UP000189981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22385 {ECO:0000313|Proteomes:UP000189981};
RA Varghese N., Submissions S.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUYR01000002; SKB73239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5DNK8; -.
DR STRING; 572036.SAMN05661099_2470; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000189981; 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:0051301; P:cell division; IEA:UniProtKB-KW.
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; 3.40.1690.20; -; 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; PTHR43655:SF39; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 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}; Cell cycle {ECO:0000313|EMBL:SKB73239.1};
KW Cell division {ECO:0000313|EMBL:SKB73239.1};
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|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:UP000189981};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 154..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 245..385
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 677..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 253..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 480
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 552
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 696 AA; 77371 MW; 9A152B8E513D0489 CRC64;
MKEDKSDTKK PLKKIPGKKI VPKTPKFNIM WLYAIIILGL FVVQYMFSGN SAQLINYQKF
ENEMLKAGDV EKLVAYKNAD LYNVDVYIKK DRLDLPKYKD LKSKNSLTGA STGPQYYFTQ
ATFESFETKI KEAEKDIPVD QHVSIVTESR ESPWAGWLMS FILPVLLLVG FWVFIMKRMG
GGAGGGGGGQ IFNIGKSKAT LFDKESQVTI TFNDVAGLEE AKQEVMEIVD FLKNPKKYTN
LGGKIPKGAL LIGAPGTGKT LMAKAVAGEA QVPFFSLSGS DFVEMFVGVG ASRVRDLFKQ
AKDKAPCIIF IDEIDAIGRA RGKNNIVGGN DERENTLNQL LVEMDGFGTD SGIIILAATN
RPDVLDTALL RPGRFDRQIS IDKPDLVGRE QIFKVHLKPL KLAEGVDAKK LSAQTPGFAG
AEIANVCNEA ALIAARRNKE AVDMQDFQDA VDRVIGGLEK KNKIISPEEK RIVAYHEAGH
AIAGWFLEHA DPLVKVSIVP RGVAALGYAQ YLPKEQFLYT TEQLLDGMCM TLGGRVAEDI
VFNKISTGAQ NDLERITKLS YAMVTIYGMN DKVGNVSFND TQGEYQFNKP YSEKTSEMID
IEVRNQIDLA YQRTKQLLTD KRDGLEKLAE KLLEKEILFQ SDLEEILGKR PFDNRTTYDE
FVNGIEPSND IPKETLQHEG VADHNIDLPE NRSTLD
//
