FTSH2_SALRM
ID FTSH2_SALRM Reviewed; 683 AA.
AC D5HA94;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=ATP-dependent zinc metalloprotease FtsH 2 {ECO:0000255|HAMAP-Rule:MF_01458};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_01458};
GN Name=ftsH2 {ECO:0000255|HAMAP-Rule:MF_01458}; OrderedLocusNames=SRM_02028;
OS Salinibacter ruber (strain M8).
OC Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC Rhodothermaceae; Salinibacter.
OX NCBI_TaxID=761659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8;
RG Genoscope;
RT "Genome sequence of Salinibacter ruber M8.";
RL Submitted (APR-2010) 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: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; FP565814; CBH24949.1; -; Genomic_DNA.
DR RefSeq; WP_011404557.1; NC_014032.1.
DR AlphaFoldDB; D5HA94; -.
DR SMR; D5HA94; -.
DR EnsemblBacteria; CBH24949; CBH24949; SRM_02028.
DR KEGG; srm:SRM_02028; -.
DR PATRIC; fig|761659.10.peg.2204; -.
DR HOGENOM; CLU_000688_16_2_10; -.
DR OMA; QVMQFGQ; -.
DR OrthoDB; 190468at2; -.
DR Proteomes; UP000000933; 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 Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..683
FT /note="ATP-dependent zinc metalloprotease FtsH 2"
FT /id="PRO_0000400389"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 50..136
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 158..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 451
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 683 AA; 74485 MW; E6F2A79F5A69E538 CRC64;
MADQTSQNDN QNGSGLPGGG PSGTGRGRLI IWVIAGTLLA LWAYSYWGMG ASGGERISYS
EFRTQLQQEN VERVEVKGNA INGSLKSQAT RSEQGNTIEY QNFVTYLPSF GDEQLMDLLE
SQGVNVVTKP ESSFPWGLVI MGLLPVLLLF GVGYIFLRRM QSQGQGLFSV RQSKAELYDK
DEEDTTFDDV AGADSAKEEL REIIKFLKNP KRFEGLGGKV PKGVLLVGPP GTGKTLLARA
VAGEANAPFF SVSGSDFMEM FVGVGASRVR DMFSEAKETS PAIIFIDELD SIGRKRGAGL
GGGNDEREQT LNQLLSELDG FEENEGVIVM AATNRPDILD SALTRPGRFD RQITVDLPTK
QSRHEILKIH AREKPLSDDV DLEEIARSTP GFSGADLENL LNEAALLAGR HGHDAIQYSD
IEQARDKVMM GLKRDGMVLD DEEKKLLAYH EAGHAIVGAV LPNADPVHKV TIVPRGKAMG
VTQQLPEKDQ YLYRHDYILD RLAVIMGGRA AEELIFDTAT SGAENDLKQV RKMARKMVLD
WGMGDQFKHI SLGEDQGNVF LGDEIAKGRE YSDDTAREVD EEIRRISEDA FQRAVDTLNE
HHEAFDQLAD MLIEQEEVSG KDVLNLVNGD TDEIGHMPTT NGAAASEENG SADDHEPDEA
TVIEEDGESG EGRASGSADA SGS
