FTSH_NITOC
ID FTSH_NITOC Reviewed; 639 AA.
AC Q3JEE4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Noc_0272;
OS Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB
OS 11848 / C-107).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Nitrosococcus.
OX NCBI_TaxID=323261;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107;
RX PubMed=16957257; DOI=10.1128/aem.00463-06;
RA Klotz M.G., Arp D.J., Chain P.S.G., El-Sheikh A.F., Hauser L.J.,
RA Hommes N.G., Larimer F.W., Malfatti S.A., Norton J.M., Poret-Peterson A.T.,
RA Vergez L.M., Ward B.B.;
RT "Complete genome sequence of the marine, chemolithoautotrophic, ammonia-
RT oxidizing bacterium Nitrosococcus oceani ATCC 19707.";
RL Appl. Environ. Microbiol. 72:6299-6315(2006).
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; CP000127; ABA56802.1; -; Genomic_DNA.
DR RefSeq; WP_002814302.1; NC_007484.1.
DR AlphaFoldDB; Q3JEE4; -.
DR SMR; Q3JEE4; -.
DR STRING; 323261.Noc_0272; -.
DR EnsemblBacteria; ABA56802; ABA56802; Noc_0272.
DR KEGG; noc:Noc_0272; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_6; -.
DR OMA; RRSNGMP; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000006838; 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..639
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400365"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 37..123
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 145..639
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 443
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 518
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 639 AA; 70244 MW; A5F12B046B57586D CRC64;
MDNEKQASPP PAAPPLNWRY LLWIILLGIF LISWLGNAGR QAGDEITYTE FKQALHQGKI
AKVTLEGQHI SGTYHEAGGN IQPEGKDSKG FSTTRPPFDD PELMKLLEQK GVVVQAKSEE
PSLWMQAIIG ILPWFLILGL IFYVSYRMQQ RMMGGGRGGP FGFGKAPVKR FREGSIGVTF
EDVAGVENAK RDLREIVDYL KEPGQFKAVG AKIPKGILLV GRPGTGKTLL ARAVAGEAGV
PFYSISGSDF IEMFVGVGAA RVRDMFKAAK EEAPSILFID EIDSVGRARG TGLGGGHDER
EQTLNQILGE MDGFAAHENV VVLAATNRPD VLDPALLRPG RFDRKVVLDL PDKKARQRVL
EVHTKNVPLA ADVDLERVAR RTVGFSGADL ANLVNEAALL TGRERKKEVD MDMFNLARDK
IVLGAKRETI LGEEEKKLVA YHESGHALTA WLLPEADPLH QVSIIPRGMA LGVTEQAPEE
ERHSLSRAYL LDRLGVMLGG RISEKITFGD VTSGAESDLK QATQLARRMV CQWGMSDKIG
AAAFSRSEEH VFLGRELSQP RDFSEQTAQI IDDEIRRILS EVERKTENLL QENRAKLDAL
AKALIEAETL NLVEVEKIFK NVKELPQEGH NEAVATGAG
