FTSH_OPITP
ID FTSH_OPITP Reviewed; 614 AA.
AC B1ZMG6;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Oter_0128;
OS Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1).
OC Bacteria; Verrucomicrobia; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX NCBI_TaxID=452637;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11246 / JCM 15787 / PB90-1;
RX PubMed=21398538; DOI=10.1128/jb.00228-11;
RA van Passel M.W., Kant R., Palva A., Copeland A., Lucas S., Lapidus A.,
RA Glavina del Rio T., Pitluck S., Goltsman E., Clum A., Sun H., Schmutz J.,
RA Larimer F.W., Land M.L., Hauser L., Kyrpides N., Mikhailova N.,
RA Richardson P.P., Janssen P.H., de Vos W.M., Smidt H.;
RT "Genome sequence of the verrucomicrobium Opitutus terrae PB90-1, an
RT abundant inhabitant of rice paddy soil ecosystems.";
RL J. Bacteriol. 193:2367-2368(2011).
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; CP001032; ACB73419.1; -; Genomic_DNA.
DR AlphaFoldDB; B1ZMG6; -.
DR SMR; B1ZMG6; -.
DR STRING; 452637.Oter_0128; -.
DR PRIDE; B1ZMG6; -.
DR EnsemblBacteria; ACB73419; ACB73419; Oter_0128.
DR KEGG; ote:Oter_0128; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_0; -.
DR OMA; PNSATAC; -.
DR Proteomes; UP000007013; 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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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..614
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_5000335214"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 27..127
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 149..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 437
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 513
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 614 AA; 66045 MW; C69E9CEBD491CD81 CRC64;
MLPIRWFLAL LAVFLAVAGL DLWFSQTGAR PSSATGEERL DGAAFLAAAN AGELREGHIV
YRANSTGLAD LHAQRKGAAG AGATHVRATA RLTDAEVTAL RTQHFAEDDP VSYAAARAVS
ARERTASIVH AIVHPLGLIT LIVGILFVVQ RYAGRFTAFS AQRLRPVTSG VSFSSVAGCD
EAKDEVYEVV EFLRDPARFR QTGGRMPKGV LLVGPPGTGK TMLAKAVAGE ARANFYSLSG
SDFVELYVGV GASRVRSLFK KARETAPSII FIDEIDAIGR QRSAAESGGA QQEHDQTLNA
LLVAMDGFDS DDAVVVFGAT NRPDTMDRAL LRPGRFDRQV SVGLPDLRGR LAILQVHAGS
VKLDPSVDLQ EIAKATPGFS GADLANLLNE GAIHAARHRR ATILHSDLDE ARDKINWGRE
TRRVMTVQDK AVIAYHEAGH ALMQVLSGED VVRVQKVTII PRGRSLGSTH FTPERDLFNY
SQPQLIAKLR CLMAGRVAEE IALGSITSGA SGDIQEATKT ARQMVLEWGM SPLGFMALSR
PDGDEPLASP QTFHEAERHV RALLDENYAA TTRALTTHRA ALDAIADELI RCETILGNDV
RRIAAQHPPS ALAG
