ID A0A2Y9BES0_9FIRM Unreviewed; 615 AA.
AC A0A2Y9BES0;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 {ECO:0000256|HAMAP-Rule:MF_01458};
GN ORFNames=A8806_104200 {ECO:0000313|EMBL:PWJ30330.1},
GN SAMN05216536_104200 {ECO:0000313|EMBL:SSA55321.1};
OS Faecalicatena orotica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Faecalicatena.
OX NCBI_TaxID=1544 {ECO:0000313|EMBL:SSA55321.1, ECO:0000313|Proteomes:UP000251306};
RN [1] {ECO:0000313|EMBL:SSA55321.1, ECO:0000313|Proteomes:UP000251306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:SSA55321.1,
RC ECO:0000313|Proteomes:UP000251306};
RA Cai Z.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PWJ30330.1, ECO:0000313|Proteomes:UP000245845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLAE-zl-C242 {ECO:0000313|EMBL:PWJ30330.1,
RC ECO:0000313|Proteomes:UP000245845};
RA Kelly W.;
RT "The Hungate 1000. A catalogue of reference genomes from the rumen
RT microbiome.";
RL Submitted (MAY-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; QGDL01000004; PWJ30330.1; -; Genomic_DNA.
DR EMBL; UETE01000004; SSA55321.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Y9BES0; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000245845; Unassembled WGS sequence.
DR Proteomes; UP000251306; Unassembled WGS sequence.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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|HAMAP-Rule:MF_01458,
KW ECO:0000256|RuleBase:RU003651}; Cell cycle {ECO:0000313|EMBL:SSA55321.1};
KW Cell division {ECO:0000313|EMBL:SSA55321.1};
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:UP000245845};
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 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 110..132
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 196..335
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT ACT_SITE 427
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 204..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 430
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 615 AA; 67978 MW; 10389CE2E841AE77 CRC64;
MNNKKYRSAG GATFLTFIVI VFLALWLTNR MQVREQDMTY TSFVQEVKDK NVQDVTIKQN
KTVPTGVVTV TLKDSDTTKQ VNVSDVNSVQ ALLEKYNIDY QMPNVQEDSW LTTILMPLLF
TFLGITLIFM FMNRQGGGAN AKAMNFGKSR AKMSTDTDKK VTFADVAGLK EEKEALEEIV
DFLKSPKKYI QVGARIPKGV LLEGPPGTGK TLLAKAVAGE AGVPFFSISG SDFVEMFVGV
GASRVRDLFQ DAKKNAPCIV FIDEIDAVAR RRGSGLGGGH DEREQTLNQL LVEMDGFGVN
EGIIVMAATN RKDILDPAIL RPGRFDRNVI VGRPDVGGRE EILKVHAKNK PLGDDVDLKQ
IAQTTSGFTG ADLENLLNEA AILSAKEGRV YLQQSDIRHA FIKVGIGPEK KSRIVSEKDR
RITAYHEAGH AILFHVLPDV GPVYSVSIIP TGGAGGYTMP LPENDDMFNT KGKMLQEITV
SLGGRVAEEE IFDDITTGAS QDIKQATAIA KSMITKFGMS ERLGLINYDN DSDEVFIGRD
FGHTSRGYGE KVASTIDEEV KRIIDECYLK ARSILKEYDS VLQNCAELLL KKEKITRSEF
EALFEEYEKW GKSFQ
//
