ID A0A0Q8MR23_9HYPH Unreviewed; 643 AA. AC A0A0Q8MR23; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 03-MAY-2023, entry version 34. 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=ASE04_08945 {ECO:0000313|EMBL:KRB51660.1}; OS Rhizobium sp. Root708. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium. OX NCBI_TaxID=1736592 {ECO:0000313|EMBL:KRB51660.1, ECO:0000313|Proteomes:UP000051238}; RN [1] {ECO:0000313|EMBL:KRB51660.1, ECO:0000313|Proteomes:UP000051238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root708 {ECO:0000313|EMBL:KRB51660.1, RC ECO:0000313|Proteomes:UP000051238}; RA Gilbert D.G.; RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KRB51660.1, ECO:0000313|Proteomes:UP000051238} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Root708 {ECO:0000313|EMBL:KRB51660.1, RC ECO:0000313|Proteomes:UP000051238}; RA Schulze-Lefert P.; RT "Functional overlap of the Arabidopsis leaf and root microbiotas."; 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:KRB51660.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LMHV01000040; KRB51660.1; -; Genomic_DNA. DR RefSeq; WP_056820649.1; NZ_LMHV01000040.1. DR AlphaFoldDB; A0A0Q8MR23; -. DR STRING; 1736592.ASE04_08945; -. DR EnsemblBacteria; KRB51660; KRB51660; ASE04_08945. DR OrthoDB; 9809379at2; -. DR Proteomes; UP000051238; 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 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 TIGRFAMs; TIGR01241; FtsH_fam; 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:KRB51660.1}; KW Cell division {ECO:0000313|EMBL:KRB51660.1}; 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|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 106..126 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 190..329 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 600..643 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 421 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 198..205 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 420 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 424 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 498 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 643 AA; 70251 MW; D9E22AEFC98774A4 CRC64; MNPNLRNFAL WAIIALLLIA LFSMFQTSPA QTSSRDIPYS QFLREVDAGR VKEVVVTGNR VSGSYIENGT TFQTYTPVVD DNLLDRLQSK NVLVSARPET DGSSGFLSYL GTLLPMLLIL GVWLFFMRQM QGGSRGAMGF GKSKAKLLTE AHGRVTFDDV AGVDEAKQDL EEIVEFLRDP QKFQRLGGKI PRGVLLVGPP GTGKTLLARS VAGEANVPFF TISGSDFVEM FVGVGASRVR DMFEQAKKNA PCIIFIDEID AVGRHRGAGL GGGNDEREQT LNQLLVEMDG FEANEGIILI AATNRPDVLD PALLRPGRFD RQVVVPNPDI IGRERILKVH ARNVPLAPNV DLKVLARGTP GFSGADLMNL VNEAALMAAR RNKRVVTMAE FEDAKDKIMM GAERRSSAMT EAEKKLTAYH EAGHAITALK VPVADPLHKA TIIPRGRALG MVMQLPEGDR YSMSYKWMVS RLVIMMGGRV AEELTFGKEN ITSGASSDIE QATKLARAMV TQWGFSDALG QVAYGENQQE VFLGHSVSQS KNVSEATAQT IDTEVRRLID EAYQEARRIL TDHHDEFVAI AEGLLEYETL TGEEIKALIR GEKPSRDLGD DTPPSRGSAV PKTGTRPASK GDEPESGLEP QTH //