FTSH_SULNB
ID FTSH_SULNB Reviewed; 671 AA.
AC A6QBN8;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=SUN_1953;
OS Sulfurovum sp. (strain NBC37-1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Sulfurovum; unclassified Sulfurovum.
OX NCBI_TaxID=387093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBC37-1;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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:0000255|HAMAP-
CC Rule:MF_01458}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01458};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01458};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase family.
CC {ECO:0000255|HAMAP-Rule:MF_01458}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000255|HAMAP-Rule:MF_01458}.
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DR EMBL; AP009179; BAF72897.1; -; Genomic_DNA.
DR RefSeq; WP_012083718.1; NC_009663.1.
DR AlphaFoldDB; A6QBN8; -.
DR SMR; A6QBN8; -.
DR STRING; 387093.SUN_1953; -.
DR EnsemblBacteria; BAF72897; BAF72897; SUN_1953.
DR KEGG; sun:SUN_1953; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_7; -.
DR OMA; NDGRAWM; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000006378; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 1.20.58.760; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF140990; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Metal-binding; Metalloprotease; Nucleotide-binding; Protease;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..671
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400400"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 44..130
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 152..671
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 630..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 448
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 224..231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 447
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 671 AA; 73403 MW; BB48703DAC7B2700 CRC64;
MANPNNNNDN KQNNNNNFFN DNPLLAFAIF SIVIILIFKS FVGEGESLGT MMNTQGVAQT
KQVKYSEIKK RIEEGAVKSV KLTPSMVEAI IEDNGRKVRY VAQNVPTYDR DLIPLLDKKK
ISYEGVVGNG FFSELISMML PILIFFAIWI FLAKKMSKGM GGGILGAGKA DKLINSEKPD
TRFDDVQGVE EAKDEVKEIV DFLKFPERYI ELGAKIPKGV LLVGPPGTGK TLLAKAVAGE
ASVPFFSVSG SGFIEMFVGV GASRVRDLFA QAKKEAPSII FIDEIDAIGK SRASGGQMGG
NDEREQTLNQ LLAEMDGFGT DTPVIVLAAT NRPETLDAAL LRAGRFDRQV LVDKPDFEGR
LAILKVHSKD VKLAPNVDLE IVAKQTAGLA GADLANIINE AALLAGRQNK KQIEQSDLLE
AIERSFVGLE KKNRKINETE KKIVAYHESG HALMSELSEG ATRVTKVSII PRGLGALGYT
LHLPEDEERF LKQKHELMAE VDVLLGGRAA EDVFIGEIST GAGNDLDRAT AILKDMVSVY
GMTDVAGLMV LSRSQNSFLG AGAVSTDYSD KTAEAMDSYI KSTLNERYGY VKETLQNYYG
AIDNMAKELL GTEVIEGKTV RRIIEEYEQE KGMPSRLAHK DKVAKNKAEA DKKEEALKKE
ISEESDNNKE A
