ID A0A3N5Y545_9ALTE Unreviewed; 649 AA.
AC A0A3N5Y545;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-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 ECO:0000313|EMBL:RPJ68790.1};
GN ORFNames=DRW07_05200 {ECO:0000313|EMBL:RPJ68790.1};
OS Alteromonas sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=2259342 {ECO:0000313|EMBL:RPJ68790.1, ECO:0000313|Proteomes:UP000275281};
RN [1] {ECO:0000313|EMBL:RPJ68790.1, ECO:0000313|Proteomes:UP000275281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0105 {ECO:0000313|EMBL:RPJ68790.1,
RC ECO:0000313|Proteomes:UP000275281};
RA Ye M.-Q., Du Z.-J.;
RL Submitted (NOV-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:RPJ68790.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RPOK01000001; RPJ68790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5Y545; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000275281; 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; 3.30.720.210; -; 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 YME1L1; 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:UP000275281};
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 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 189..328
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 597..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 197..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 649 AA; 71319 MW; 9BEC3071F94BC6F5 CRC64;
MSDMAKNLIL WLVIAVVLMS VFQSFSPGES SKSQMDYTTF IKEVNQGMIR EVSINNSTQE
IIGQKRTGDT FKTLIPSYDA NLINDLLKQD VKVVGVPPEK PSFLANIFIS WFPMLLLIGV
WIFFMRQMQG GGGRGAMSFG KSKARLLSED QIKTTFADVA GCDEAKEDVS ELVDFLRDPS
KFQKLGGKIP KGVLMVGPPG TGKTLLAKAI AGEAKVPFFT ISGSDFVEMF VGVGASRVRD
MFEQARKSAP CIIFIDEIDA VGRQRGAGLG GGHDEREQTL NQMLVEMDGF DGHEGIIVIA
ATNRPDVLDP ALLRPGRFDR QVVVGLPDIR GREQILKVHM RKVPIADNVE AAVIARGTPG
FSGADLANLV NEAALFAARS NKRLVAMEEF EKAKDKIMMG SERKSMVMSE EEKTMTAYHE
AGHAIVGRLV PEHDPVYKVS IIPRGRALGV TMYLPEQDRV SHSKQHLESM LSSLFGGRIA
EQIIYGDDKV TTGASNDIER ATDIARKMVT QWGLSSKMGP MLYAEEEGEV FLGRSMSKAS
HMSDDTARAI DSEIKSLIDR NYERAQKILE DNIDILHAMK DALMKYETID AKQIDDLMER
RSVRPPADWD DRSGNNSSSS GGNAPKDAEM NVDEDDKKGS VGNPGDLPS
//