ID A0A1B1Q436_9CHLB Unreviewed; 654 AA.
AC A0A1B1Q436;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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_2 {ECO:0000313|EMBL:ANT65614.1};
GN Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN ORFNames=Ptc2401_01882 {ECO:0000313|EMBL:ANT65614.1};
OS Prosthecochloris sp. CIB 2401.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1868325 {ECO:0000313|EMBL:ANT65614.1, ECO:0000313|Proteomes:UP000092496};
RN [1] {ECO:0000313|EMBL:ANT65614.1, ECO:0000313|Proteomes:UP000092496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB 2401 {ECO:0000313|EMBL:ANT65614.1,
RC ECO:0000313|Proteomes:UP000092496};
RA Nabhan S., Bunk B., Sproeer C., Bryant D.A., Overmann J.;
RT "Genome Sequence of Prosthecochloris phaeum CIB2401 of the phylum
RT Chlorobi.";
RL Submitted (JUL-2016) 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}.
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DR EMBL; CP016432; ANT65614.1; -; Genomic_DNA.
DR RefSeq; WP_068867770.1; NZ_CP016432.1.
DR AlphaFoldDB; A0A1B1Q436; -.
DR STRING; 1868325.Ptc2401_01882; -.
DR KEGG; proc:Ptc2401_01882; -.
DR PATRIC; fig|1868325.3.peg.1849; -.
DR InParanoid; A0A1B1Q436; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000092496; Chromosome.
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; 3.40.50.300; 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 FTSH 2, CHLOROPLASTIC-RELATED; 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:UP000092496};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01458}; Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 242..381
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 473
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 250..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 472
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 654 AA; 72009 MW; 773F978264B31400 CRC64;
MGNNDQHKEK KGSKFRPVKD DQGEPSGWFG GGDNQTPPSS GVPKIFIYVL IGLMAVFIFQ
RFFVSTAGPE TSYNEYRSML EKGGVAAVTV ETYPDGSALL AVRLRTQATV RMTDGSTVMT
DNFSVRVPEF SLEQAEQLAL KEIEVNVRPG GDGLENFLIL MAPWIIFAFI YFFIFRRMSA
QNGGAQKNIF SFGKSRAKLM SDFDVKVKFE DVAGVDEAVE ELKETVEFLM SPEKFEKIGG
KIPKGVLLLG PPGTGKTLLA KAIAGEAQVP FFSISGADFV EMFVGVGAAR VRDLFETAKK
NAPCIVFIDE IDAVGRSRGA GLGGGHDERE QTLNQLLVEM DGFATKDNVI LIAATNRPDV
LDTALLRPGR FDRQITIDKP DIRGREAILA IHARKTPLSK EVDLKSIAQS TPGFSGADLA
NLINEAALLA SREGREDIST QNFDDARDKI LMGPERRSMY ISDAQKKITA YHESGHVLVA
KFTEGSDPIH KVTIIPRGRS LGQTAYLPVE DRYTQNREYL IAIITYALGG RVAEELILKE
TSTGAANDIE KATDIARKMV RNWGMSEKLG PINYGDGHKE VFLGKDYSHV REYSEETALQ
IDVEVRNIIM ECMQNAKRIL TDHTASLHAL AEALVEKESL SGEEIDRIIT AAQH
//
