ID A0A0F3MEQ3_ORITS Unreviewed; 627 AA.
AC A0A0F3MEQ3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=hflB {ECO:0000313|EMBL:KJV54220.1};
GN Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458,
GN ECO:0000313|EMBL:SPR13238.1};
GN ORFNames=GILLIAM_02734 {ECO:0000313|EMBL:SPR13238.1}, OTSGILL_0046
GN {ECO:0000313|EMBL:KJV54220.1};
OS Orientia tsutsugamushi str. Gilliam.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Orientia.
OX NCBI_TaxID=1359184 {ECO:0000313|EMBL:KJV54220.1, ECO:0000313|Proteomes:UP000033769};
RN [1] {ECO:0000313|EMBL:KJV54220.1, ECO:0000313|Proteomes:UP000033769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gilliam {ECO:0000313|EMBL:KJV54220.1,
RC ECO:0000313|Proteomes:UP000033769};
RA Daugherty S.C., Su Q., Abolude K., Beier-Sexton M., Carlyon J.A.,
RA Carter R., Day N.P., Dumler S.J., Dyachenko V., Godinez A., Kurtti T.J.,
RA Lichay M., Mullins K.E., Ott S., Pappas-Brown V., Paris D.H., Patel P.,
RA Richards A.L., Sadzewicz L., Sears K., Seidman D., Sengamalay N.,
RA Stenos J., Tallon L.J., Vincent G., Fraser C.M., Munderloh U.,
RA Dunning-Hotopp J.C.;
RT "Genome Sequencing of Rickettsiales.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPR13238.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gilliam {ECO:0000313|EMBL:SPR13238.1};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000244959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gilliam {ECO:0000313|Proteomes:UP000244959};
RA Batty M. E., Batty M E.;
RL Submitted (MAR-2018) 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; LANO01000001; KJV54220.1; -; Genomic_DNA.
DR EMBL; LS398551; SPR13238.1; -; Genomic_DNA.
DR RefSeq; WP_047220069.1; NZ_LS398551.1.
DR PATRIC; fig|1359184.3.peg.54; -.
DR Proteomes; UP000033769; Unassembled WGS sequence.
DR Proteomes; UP000244959; Chromosome i.
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; 3.30.720.210; -; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01458}; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01458};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
KW Reference proteome {ECO:0000313|Proteomes:UP000244959};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 188..327
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT ACT_SITE 419
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 196..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 496
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 627 AA; 69037 MW; 845D615EED294ECD CRC64;
MNNQNRNVLF WATVFIVLVV AFNLLQGESF ITSQQQLHLS DFLARVDAKQ VSRVKIQGHS
LEGELTDGSS FSTYFGNYDN LVNRLNDNGV HIEVLPTSTR MGAFISTIIS WFPMLLFIGV
WIFVMRQMQS GSSKALYFGR SKAKLMAENS VRVSFKDVAG IEEAKDELME IVDFLRDPGK
FQKLGGKIPK GCLLIGPPGT GKTLLAKAIA GEANVPFFHI SGSNFVEMFV GVGASRVRDM
FEQAKKNAPC IVFIDEIDAV GRHRGIGLGG GNDEREQTLN QILVEMDGFE SNEGVIVVAA
TNRADVLDQA LLRPGRFDRK IVLINPDVKG REKILNVHLQ KVKHAADVNI KAIACGTFGL
SGAALANIVN ESALIAAKNN KKEISNEDLE QAKDKIMMGS ERRSMALTDE QKRCTAYHEA
GHAIVALYVK ASDPIHKVTI VPRGSSLGMV MRLPEHDRLN YTKEQLESNI AVALGGRIAE
EVIFGKEKVT TGAAEDIKQC TKIARFMVLE AGLSDKVGLQ EYTSYYESSS YPNQRGKLAF
MSEKNAQMIE DEVTRLINTG YTLAREIITS HSDKLELIAN SLLDKETLNG NDVKLLVFGE
QKTKVKKKNS QSKIKIASEK NDEAAAG
//
