FTSH_LANP1
ID FTSH_LANP1 Reviewed; 644 AA.
AC C8W731;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=Apar_0842;
OS Lancefieldella parvula (strain ATCC 33793 / DSM 20469 / CCUG 32760 / JCM
OS 10300 / KCTC 3663 / VPI 0546 / 1246) (Atopobium parvulum).
OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Lancefieldella.
OX NCBI_TaxID=521095;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33793 / DSM 20469 / CCUG 32760 / JCM 10300 / KCTC 3663 / VPI
RC 0546 / 1246;
RX PubMed=21304653; DOI=10.4056/sigs.29547;
RA Copeland A., Sikorski J., Lapidus A., Nolan M., Del Rio T.G., Lucas S.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Pukall R., Chertkov O.,
RA Brettin T., Han C., Detter J.C., Kuske C., Bruce D., Goodwin L.,
RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K.,
RA Chain P., Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Atopobium parvulum type strain (IPP 1246).";
RL Stand. Genomic Sci. 1:166-173(2009).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01458};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458};
CC 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; CP001721; ACV51271.1; -; Genomic_DNA.
DR AlphaFoldDB; C8W731; -.
DR SMR; C8W731; -.
DR STRING; 521095.Apar_0842; -.
DR PRIDE; C8W731; -.
DR EnsemblBacteria; ACV51271; ACV51271; Apar_0842.
DR KEGG; apv:Apar_0842; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_11; -.
DR OMA; YDKQGGG; -.
DR Proteomes; UP000000960; 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 membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Nucleotide-binding; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..644
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400327"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 35..117
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 139..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT ACT_SITE 446
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 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 449
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 522
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 644 AA; 70420 MW; CE5CF742E447CCF5 CRC64;
MANNDNKHRR SMSMLLYIAV AIFVYLLLSN TLLPGLLRQQ IQTVSYSEFL NKIESNEVTK
VDLNTGNRNI RFTTGSGDSE KIFETTQFPN DSTLVQTLRE HKVDFSASIP DNSANMLMYA
LIQYGIPLII FLGIGFFINR SLKRAMGDDG PSMNFGGGFG GLGGNLGRSS AKEIKGEDTG
ITFKDVAGQE EAKESMQEIV SFLKTPDKYK EIGARCPRGA LLVGPPGTGK TLIAKAVAGE
AGVPFFQIAG SEFVEMFVGR GAAKVRDLFK QANEKAPCII FIDEIDAVGK RRDASLNSND
EREQTLNQLL SEMDGFDNHK GIVVLAATNR PETLDKALLR PGRFDRRIPV ELPDLKGREA
VLQIHANDVK MEPGVDLSIV AKSTPGASGA DLANIINEAA LRAVRFGRRR VTTEDLTESV
DVVIAGAKKK NSVLSEHEKD VVAYHETGHA IVGAIQKNDA PVTKITIVPR TSGALGFTMQ
VEDDERYLMS KSQAMDEIAV LCGGRAAEEL IFGEMTNGAS NDIERATAIA RAMVTQYGMS
DKLGMVTLSQ QQSRYLGGGS SLTCSEATAE EIDAEVRRIV EEGHQRALQT LKENRFKLHE
IAHYLQKKET ITGEEFMNIL KRENTFAPVD KNINDEGSST PSEE
