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Database: UniProt
Entry: A0A1M4WYK4_9GAMM
LinkDB: A0A1M4WYK4_9GAMM
Original site: A0A1M4WYK4_9GAMM 
ID   A0A1M4WYK4_9GAMM        Unreviewed;       640 AA.
AC   A0A1M4WYK4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN02745148_01252 {ECO:0000313|EMBL:SHE86143.1};
OS   Halomonas ilicicola DSM 19980.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1121942 {ECO:0000313|EMBL:SHE86143.1, ECO:0000313|Proteomes:UP000184346};
RN   [1] {ECO:0000313|EMBL:SHE86143.1, ECO:0000313|Proteomes:UP000184346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19980 {ECO:0000313|EMBL:SHE86143.1,
RC   ECO:0000313|Proteomes:UP000184346};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQUJ01000005; SHE86143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M4WYK4; -.
DR   STRING; 1121942.SAMN02745148_01252; -.
DR   OrthoDB; 9809379at2; -.
DR   Proteomes; UP000184346; 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 YME1L1; 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:SHE86143.1};
KW   Cell division {ECO:0000313|EMBL:SHE86143.1};
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:UP000184346};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   TRANSMEM        37..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   TRANSMEM        141..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          229..368
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        459
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         237..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         458
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         462
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         534
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   640 AA;  71472 MW;  7642B1D0CF9C0ACA CRC64;
     MAFWNRDKGR QRQETSDWSS SGFDPQEEFQ QRVRRRWVLF FWISLAILAL FYVLDIQRQP
     ERSNLTYGQF LQAVDSGHVE AVTLRGQRIE GRLSQAGREA LEAATSETFE TVRPTLAGEP
     LLQRLEAQGI TITAEPTEAP WWQRILVGAL PWILILGLLL WFWGRMQQRM MSGGGPFGLG
     QSKAKKIQRE DTDARLVDVA GSENAKQEIT EVIDFLKQPS RFHALGAKIP HGILMMGPPG
     TGKTLMARAV AGEANVPFFS ISGSEFIEMF VGVGASRVRD LFKQAREQAP AVIFIDELDS
     IGRSRGAGMG GGHDEREQTL NQILSQMDGF EAEESVVVLA ATNRPDVLDP ALLRPGRFDR
     KITFDLPHRK ARQAILEVHT KNMPLAEDVN LGHLAEITIG FSGADLANLA NEAALYAGRR
     EQQEVDWACF TDARDRLMLG EAREAVLAES ERHIIAYHES GHALLAYLLP HADPLEKVTV
     IPRGRALGAT AQTPDEERYN FNEAYLRDRI AVMFGGRLAE SLVFGQVSSG AEDDLKQATQ
     LARRMVAHWG MNERIGPASF PQSEQQVFLA KEISQGREHS EATAAIIDEE IRKLLGNIEA
     QARDLLETHR RHLDDLASAL EKQETLEAAE IHRILDNVDR
//
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