ID A0A0Q8MR23_9RHIZ Unreviewed; 643 AA. AC A0A0Q8MR23; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 20-JUN-2018, entry version 16. 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; 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 Millard Andrew; 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 Vorholt J.; 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 CC metallopeptidase for both cytoplasmic and membrane proteins. Plays CC a role in the quality control of integral membrane proteins. CC {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01458}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_01458}; CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_01458}; Cytoplasmic side {ECO:0000256|HAMAP- CC 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 CC M41 family. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- SIMILARITY: In the central section; belongs to the AAA ATPase CC family. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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:0016887; F:ATPase activity; IEA:UniProtKB-UniRule. 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 HAMAP; MF_01458; FtsH; 1. DR InterPro; IPR003593; AAA+_ATPase. 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; 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}; KW 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 Complete proteome {ECO:0000313|Proteomes:UP000051238}; KW Hydrolase {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|HAMAP-Rule:MF_01458}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Protease {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 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 190 329 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 198 205 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT COILED 274 294 {ECO:0000256|SAM:Coils}. FT ACT_SITE 421 421 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 420 420 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 424 424 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 498 498 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT 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 //