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Database: UniProt
Entry: A0A0W1FFB4_9SPHN
LinkDB: A0A0W1FFB4_9SPHN
Original site: A0A0W1FFB4_9SPHN 
ID   A0A0W1FFB4_9SPHN        Unreviewed;       647 AA.
AC   A0A0W1FFB4;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=ATE62_06170 {ECO:0000313|EMBL:KTE41455.1};
OS   Sphingopyxis sp. HIX.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1759074 {ECO:0000313|EMBL:KTE41455.1, ECO:0000313|Proteomes:UP000053691};
RN   [1] {ECO:0000313|Proteomes:UP000053691}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIX {ECO:0000313|Proteomes:UP000053691};
RA   Gomez-Alvarez V., Revetta R.P.;
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTE41455.1}.
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DR   EMBL; LNSB01000009; KTE41455.1; -; Genomic_DNA.
DR   RefSeq; WP_058808277.1; NZ_LNSB01000009.1.
DR   AlphaFoldDB; A0A0W1FFB4; -.
DR   STRING; 1759074.ATE62_06170; -.
DR   Proteomes; UP000053691; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01458}; Cell cycle {ECO:0000313|EMBL:KTE41455.1};
KW   Cell division {ECO:0000313|EMBL:KTE41455.1};
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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01458};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01458};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   TRANSMEM        109..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          195..334
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          603..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..619
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        426
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         203..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         503
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   647 AA;  71064 MW;  5D3CFCFB20E9A6A5 CRC64;
     MQDDKEPQGN PWMKSVMIWS GILLAMLLVA SMFGGASQPA GNALTYSEFR QKIEDGSVKD
     VVLTEERATG TLSNGDRFSA NLIRDPELLK LLNDNNVKYD GKPTETGNIW VYLLIQSLPF
     LLILGIAFFV FRQVQKNNGS GAMGFGKSRA KMLTEKQGRV TFDDVAGIDE AREELEEIVE
     FLKDPTKFSK LGGQIPKGAL LVGSPGTGKT LLARAIAGEA GVPFFTISGS DFVEMFVGVG
     ASRVRDMFEQ AKRNAPCIVF IDEIDAVGRH RGAGLGNGND EREQTLNQLL VEMDGFEANE
     GIIIVAATNR PDVLDPALLR PGRFDRQVVV PRPDIEGRQK ILEVHTRKKP LAPDVDLRRI
     ARGTPGFSGA DLANLANEAA LLAARKGKRL IASNEFEEAK DKVLMGAERR SMVMTEDEKK
     ATAYHEAGHA LVSLHVEHND PLHKVTIIPR GRALGVTWNL PERDRYSQNM KQMKARLALC
     FGGRIAEQLI YGKDELNTGA SNDIQQATDM ARAMVMEYGM SEKLGWLRYR DNQDEVFLGH
     SVSRAQNMSE ETAKLIDAEV RRLVEEGEKV ARKVLTDNLD ELHLLAAALL EYETLSGEEA
     KRAIKGEDIG REDDAGKRGT PVSGHAGGLP QIKRKPRPFG GPNPQGA
//
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