ID A0A1E3SEJ5_9MYCO Unreviewed; 743 AA. AC A0A1E3SEJ5; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 25-MAY-2022, entry version 30. 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=BHQ20_12340 {ECO:0000313|EMBL:ODR00550.1}, BST27_19975 GN {ECO:0000313|EMBL:ORA98975.1}; OS Mycobacterium intermedium. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium simiae complex. OX NCBI_TaxID=28445 {ECO:0000313|EMBL:ODR00550.1, ECO:0000313|Proteomes:UP000094976}; RN [1] {ECO:0000313|Proteomes:UP000094976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMC2_M5 {ECO:0000313|Proteomes:UP000094976}; RA Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ODR00550.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMC2_M5 {ECO:0000313|EMBL:ODR00550.1}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:ORA98975.1, ECO:0000313|Proteomes:UP000192739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 44049 {ECO:0000313|EMBL:ORA98975.1, RC ECO:0000313|Proteomes:UP000192739}; RA Tortoli E., Trovato A., Cirillo D.M.; RT "The new phylogeny of genus Mycobacterium."; RL Submitted (FEB-2017) 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:ODR00550.1}. 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; MIHB01000017; ODR00550.1; -; Genomic_DNA. DR EMBL; MVHT01000061; ORA98975.1; -; Genomic_DNA. DR RefSeq; WP_069419424.1; NZ_MVHT01000061.1. DR STRING; 28445.BHQ20_12340; -. DR EnsemblBacteria; ODR00550; ODR00550; BHQ20_12340. DR EnsemblBacteria; OPE48948; OPE48948; BV508_16140. DR EnsemblBacteria; ORA98975; ORA98975; BST27_19975. DR Proteomes; UP000094976; Unassembled WGS sequence. DR Proteomes; UP000192739; 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: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 Gene3D; 1.20.58.760; -; 1. DR Gene3D; 3.40.50.300; -; 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 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; 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:ODR00550.1}; KW Cell division {ECO:0000313|EMBL:ODR00550.1}; 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|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:UP000094976}; 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 7..26 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT TRANSMEM 115..132 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 195..334 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT NP_BIND 203..210 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT REGION 616..743 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 696..716 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 426 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 425 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 429 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT METAL 501 FT /note="Zinc; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 743 AA; 80106 MW; 54E09219105FA47E CRC64; MNRKNVLRTV TIVAVVVLLG WSFFYFSDDT RGYKPVDTSV AMQQISSDNV KSAQIDDREQ QLRLTLKKGN NETENSDKVI TKFPAGYGVD LFNALNAKNA KVNTVVNEGS ILGELLVYVL PLLLLVGLFV MFSRMQGGAR MGFGFGKSRA KQMSKDMPKT TFADVAGVDE AVEELYEIKD FLQNPSRYQA LGAKIPKGVL LYGPPGTGKT LLARAVAGEA GVPFFTISGS DFVEMFVGVG ASRVRDLFEQ AKQNSPCIIF VDEIDAVGRQ RGAGLGGGHD EREQTLNQLL VEMDGFGDRA GVILIAATNR PDILDPALLR PGRFDRQIPV SNPDLAGRRA VLRVHSKGKP IAEDADLDGL AKRTVGMTGA DLANVINEAA LLTARENGTV ITSAALEEAV DRVIGGPRRK GRIISEQEKK ITAYHEGGHT LAAWAMPDID PVYKVTILAR GRTGGHAVAV PEEDKGLRTR SEMIAQLVFA MGGRAAEELV FREPTTGAVS DIEQATKVAR AMVTEYGMSA RLGAVKYGTE HGDPFLGRTM GTQPDYSHEV AGAIDEEVRK LIEAAHTEAW EILTEYRDVL DTLAGELLEK ETLHRPELEG IFAGVEKRPR LTMFDDFGGR IPSDKPPIKT PGELAMERGE PWPPEPVPEP PFKVAIARAE AAKAAEGESG GNGANGSPAA GAKPTQPDYG APAGWHAPGW PPPPGRQTPY QPYPPSDQSK PDTDESSERS GKDVSRSNPP AHG //