ID A0A0Q8MR23_9RHIZ Unreviewed; 643 AA. AC A0A0Q8MR23; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 07-APR-2021, 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=ASE04_08945 {ECO:0000313|EMBL:KRB51660.1}; OS Rhizobium sp. Root708. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae; OC 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 EnsemblBacteria; KRB51660; KRB51660; ASE04_08945. DR Proteomes; UP000051238; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; 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 Gene3D; 1.20.58.760; -; 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 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; SSF140990; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 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:KRB51660.1}; KW Cell division {ECO:0000313|EMBL:KRB51660.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Coiled coil {ECO:0000256|SAM:Coils}; 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" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 198..205 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT REGION 600..643 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 274..294 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 421 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 420 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 424 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 498 FT /note="Zinc; 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 //