FTSH_AKKM8
ID FTSH_AKKM8 Reviewed; 812 AA.
AC B2UMY1;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Amuc_0348;
OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC
OS 81048 / CCUG 64013 / CIP 107961 / Muc).
OC Bacteria; Verrucomicrobia; Verrucomicrobiae; Verrucomicrobiales;
OC Akkermansiaceae; Akkermansia.
OX NCBI_TaxID=349741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP
RC 107961 / Muc;
RX PubMed=21390229; DOI=10.1371/journal.pone.0016876;
RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M.,
RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.;
RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin
RT degrader, and its use in exploring intestinal metagenomes.";
RL PLoS ONE 6:E16876-E16876(2011).
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; CP001071; ACD04187.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UMY1; -.
DR SMR; B2UMY1; -.
DR STRING; 349741.Amuc_0348; -.
DR MEROPS; M41.021; -.
DR EnsemblBacteria; ACD04187; ACD04187; Amuc_0348.
DR KEGG; amu:Amuc_0348; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_347392_0_0_0; -.
DR Proteomes; UP000001031; 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; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 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..812
FT /note="ATP-dependent zinc metalloprotease FtsH"
FT /id="PRO_0000400321"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 43..241
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT TOPO_DOM 263..812
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT REGION 739..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..792
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 556
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 333..340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
FT BINDING 631
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01458"
SQ SEQUENCE 812 AA; 89455 MW; 647EFBF438F5D0C6 CRC64;
MPPSPPRPPK FPGSGRPESP NWGVWVMVLL IVGVLAFGFF TPESFGLGPR KENLESFEAQ
YKAGRVVLND PKAPVEVVLS ENGSEGVIHA LVYRKEIQPK VEMTPFALTY SMSLPDRDKP
LLNELSGYRV VESPYRTEEG KNVSLIPEGA QKLSVPEFNR LALEGRIAGG KDGIILAEDG
NQNVLVGQIV TRIWPAATGD ASVDKQRFER VEVPFTLEFQ GDRVKQLLGP DTKFKRESGS
WGGILLNLLP IVLILVILFF MFRAQSGGAR GAMSFGKSRA RLISPDKNKV TFKDVAGISE
AKEEVWELVE FLRNPEKFRD LGATIPRGVL MVGAPGTGKT LLARAIAGES NASFYSISGS
DFVEMFVGVG ASRVRDMFEQ AKRTAPSLIF IDEIDAVGRQ RGYGMGGGND EREQTLNALL
VEMDGFENNS NVIVIAATNR ADILDPALLR PGRFDRQVVV NLPDVRGREQ ILQVHARKVK
MAPGVSFERI ARGTSGFSGA QLANLVNEAA LLAARKGLKE ITEAELEEAR DKVSWGRERR
SLAINERGRR ITAVHEAGHA ICLLKTPHSE PLHRVTIVPR GGALGMTMWL PSDDKMHQLR
SEMLDQLVVA MGGRCAEQIV FGDVTSGATG DIKSATNLAR RMVCEFGMSE KLGLIEYGEH
QGEVYIARDL GTRSRNYSES TAELIDSEVR FLVDSAYERA MAILTENRDK LDILTEALME
FETLEGSQVM DILEYGEMKN PPARVTPPPM PSEVEEQPGK DDSGHNEKKE AEETRADGAE
ERKMEEELEQ AERAPFSYNP VDEFGKDGGE KK
