ID A0A0D4C184_9MICC Unreviewed; 710 AA.
AC A0A0D4C184;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=UM93_14185 {ECO:0000313|EMBL:AJT42353.1};
OS Psychromicrobium lacuslunae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Psychromicrobium.
OX NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT42353.1, ECO:0000313|Proteomes:UP000061839};
RN [1] {ECO:0000313|EMBL:AJT42353.1, ECO:0000313|Proteomes:UP000061839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT42353.1,
RC ECO:0000313|Proteomes:UP000061839};
RX PubMed=25908143;
RA Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter sp.
RT Strain IHBB 11108 Using PacBio Single-Molecule Real-Time Sequencing
RT Technology.";
RL Genome Announc. 3:0-0(2015).
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; CP011005; AJT42353.1; -; Genomic_DNA.
DR RefSeq; WP_045076190.1; NZ_CP011005.1.
DR AlphaFoldDB; A0A0D4C184; -.
DR STRING; 1618207.UM93_14185; -.
DR MEROPS; M41.015; -.
DR KEGG; ari:UM93_14185; -.
DR PATRIC; fig|1618207.4.peg.2882; -.
DR HOGENOM; CLU_000688_16_1_11; -.
DR OrthoDB; 9809379at2; -.
DR Proteomes; UP000061839; Chromosome.
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; 3.40.50.300; 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; 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; 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:AJT42353.1};
KW Cell division {ECO:0000313|EMBL:AJT42353.1};
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:UP000061839};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 198..337
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 623..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..644
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 432
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 504
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 710 AA; 76605 MW; 63501B58B51D5BDF CRC64;
MDIKKILKGP IVWIVVVLAL AILGFSLLNI GGSARVDTSD GISLISDQKV ESAKIYAEGR
VDLTLKEDFS KDNQNLGKNV QFFVVQDRIK DVISDLSSAK VAKYDDQPVQ NNFLASFLSL
VLPILVIGAI FWFLISRMQG GGSKVMQFGK SRAKLISKDM PQVTFADVAG ADEAVEELHE
IKEFLQEPQK FQAVGAKIPK GVLLYGPPGT GKTLLARAVA GEAGVPFYSI SGSDFVEMFV
GVGASRVRDL FEQAKANSPA IIFVDEIDAV GRHRGAGIGG GNDEREQTLN QLLVEMDGFD
VKTNVILIAA TNRPDVLDPA LLRPGRFDRQ IPVEAPDRIG REQILQVHSK GKPMAQGVDL
NAVAKKTPGY TGADLANVLN EAALLTARSN AQLIDDRALD EAIDRVMAGP QKRTRVMKER
ERKITAYHEG GHALVAAALR YSAPVTKITI LPRGRALGYT MVVPDDDKYS VTRNELLDQM
SYAMGGRVAE EIVFHDPSTG ASNDIEKATA TARKMVMEYG MSERIGAVKL GSGSGEPFLG
RDAGRERDYS EDVAATIDLE VRKLIEQAHD EAYAVLIENR DVLDRLALEL LERETLNQQE
IEEVFHDIRK RELRDIWLSA DSRPVSDIPP VVTERERRDA AAAGEPDPDS VSPQEQLASA
NLLGPSDAPG GGTGGELGQP GSGHGAPGES SETDGQLGHG SEGPAQSGSS
//
