ID A0A345HE97_9FLAO Unreviewed; 642 AA.
AC A0A345HE97;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=DVK85_11985 {ECO:0000313|EMBL:AXG74907.1};
OS Flavobacterium arcticum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1784713 {ECO:0000313|EMBL:AXG74907.1, ECO:0000313|Proteomes:UP000253951};
RN [1] {ECO:0000313|EMBL:AXG74907.1, ECO:0000313|Proteomes:UP000253951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1502 {ECO:0000313|EMBL:AXG74907.1,
RC ECO:0000313|Proteomes:UP000253951};
RA Li Y., Li D.-D.;
RT "Complete genome sequence of Flavobacterium arcticum type strain SM1502T.";
RL Submitted (JUL-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}.
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DR EMBL; CP031188; AXG74907.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345HE97; -.
DR KEGG; fat:DVK85_11985; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000253951; 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; 3.40.1690.20; -; 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; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF2; SD01613P; 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|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:UP000253951};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 221..361
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT ACT_SITE 453
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 229..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 527
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 642 AA; 71363 MW; 834AE2E3E37BD514 CRC64;
MSKDNKPSKT RINPWLIYGG ILVAFLAINF FGGDSTWNDP KPISLSKFYK FVDDNEVNKV
VFNKSTAKVY LKEDAITKKE HEEVSKDIFD KPNAGPHYTL EIGNSELFQK KLDEALQAGK
INEYNPEPES MWGDLLLTLL PILILVALWI FMMRRMSGGG AGGGGQIFNI GKSKAKLFDE
KNDIKVTFKD VAGLEGAKEE IQEIVEFLRN PEKYTNIGGK IPKGALLVGP PGTGKTLLAK
AVAGEAKVPF FSLSGSDFVE MFVGVGASRV RDLFKQAKEK SPAIIFIDEI DAVGRARGKS
NFSGSNDERE NTLNQLLTEM DGFGTNTNVI VLAATNRADV LDKALMRAGR FDRQIYVDLP
DIRERKEIFE VHLKPLKKSE ELDTDFLAKQ TPGFSGADIA NVCNEAALIA ARKDKKSVDK
QDFLDAVDRI VGGLEKKNKI ITKEEKRAIA IHEAGHATIS WMLEHAHPLV KVTIVPRGQS
LGAAWYLPEE RLIVRPEQML DEMCATMGGR AAEKVIFDKI STGALSDLEK VTKQARAMVT
IYGLNDKLGN ITYYDSSGQN EYNFSKPYSE ETARTIDEEI SILIESQYKR AIDILGDNKD
KLVKLADILI EKEVIFKDDL EDIFGKRPFD SDSTEAEVIT EA
//
