ID A0A1Q3GS48_9BACT Unreviewed; 696 AA.
AC A0A1Q3GS48;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BKI52_24750 {ECO:0000313|EMBL:OJJ18785.1};
OS marine bacterium AO1-C.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae.
OX NCBI_TaxID=1905359 {ECO:0000313|EMBL:OJJ18785.1, ECO:0000313|Proteomes:UP000186474};
RN [1] {ECO:0000313|EMBL:OJJ18785.1, ECO:0000313|Proteomes:UP000186474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-C {ECO:0000313|EMBL:OJJ18785.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-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}.
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:OJJ18785.1}.
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DR EMBL; MLAY01000008; OJJ18785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3GS48; -.
DR STRING; 1905359.BKI52_24750; -.
DR Proteomes; UP000186474; 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: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; 3.40.1690.20; -; 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; PTHR43655:SF39; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 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};
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|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:UP000186474};
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 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 238..378
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 660..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 470
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 469
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 473
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 545
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 696 AA; 77120 MW; 690D1132568913DB CRC64;
MSKNNNQKKK KIAPNNKAPQ RSGYQFWLIT VLIILIAGIA YFSKSSSAVK ITQLQFDNIL
RDGNVAKVVV INKETVEVTI KKDSLKKYSN LLKDQRMPLG SNRGPHFKFS ILDPKDFVER
FDAVQDEMIK NKKITESERI GYVPEQESDF TGLIFNWGIL FLMLFGLWFL MRRMTGGGGP
GGQIFNIGKS RAALFDAENR VKITFSDVAG LDEAKEEVKE IVEFLKHPSK YTSLGGKIPK
GALLVGPPGT GKTLLAKAVA GEAGVPFFSL SGSDFVEMFV GVGAARVRDL FKQAKEKAPC
IVFIDEIDAI GRSRGRGQMP GSNDERENTL NSLLVEMDGF STDSGVIILA ATNRPDVLDS
ALMRPGRFDR QVSIDKPDII GREAIFKVHL KPLKLANDVD SKKLAAQTPG FAGAEIANVC
NESALIAARK DKKSVDMQDF QDAIDRVIGG LEKKNKLISP SEKKIVAYHE AGHAVSGWFL
EHADPLVKVS IVPRGIAALG YAQYLPREQF LHTKEQLMDE MCMTLGGRAA EDIVFGRVST
GALSDLERIT KMAYGIVTMY GMNDKIGNVS FYDSKSSSDY SFTKPYSDAT ANTIDEEVRN
LIAECYDRTK TLLTDKREEL EIIAQELLSK EIIFQNDLER LIGKRPFDND TSYQAFTKHV
NGKHDTDDKE EEKIVNSAIQ DKDADENGSS SDTENN
//
