ID A0A1E3SEJ5_9MYCO Unreviewed; 743 AA. AC A0A1E3SEJ5; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 07-JUN-2017, entry version 6. 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}, BV508_16140 GN {ECO:0000313|EMBL:OPE48948.1}; OS Mycobacterium intermedium. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=28445 {ECO:0000313|EMBL:ODR00550.1, ECO:0000313|Proteomes:UP000094976}; RN [1] {ECO:0000313|EMBL:OPE48948.1, ECO:0000313|Proteomes:UP000190917} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMC1 {ECO:0000313|EMBL:OPE48948.1, RC ECO:0000313|Proteomes:UP000190917}; RA Greninger A.L., Jerome K., Mcnair B., Wallis C., Fang F.; RT "Genome sequences of unsequenced Mycobacterium."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ODR00550.1, ECO:0000313|Proteomes:UP000094976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HMC2_M5 {ECO:0000313|EMBL:ODR00550.1, RC ECO:0000313|Proteomes:UP000094976}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; RL Submitted (SEP-2016) 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: 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: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; MIJC01000059; OPE48948.1; -; Genomic_DNA. DR RefSeq; WP_069419424.1; NZ_MIHB01000017.1. DR EnsemblBacteria; ODR00550; ODR00550; BHQ20_12340. DR Proteomes; UP000094976; Unassembled WGS sequence. DR Proteomes; UP000190917; 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-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-HAMAP. 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; IPR000642; Peptidase_M41. DR Pfam; PF00004; AAA; 1. DR Pfam; PF01434; Peptidase_M41; 1. DR SMART; SM00382; AAA; 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:ODR00550.1}; KW Cell division {ECO:0000313|EMBL:ODR00550.1}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Complete proteome {ECO:0000313|Proteomes:UP000094976, KW ECO:0000313|Proteomes:UP000190917}; 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 7 26 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT TRANSMEM 115 132 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 195 334 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 203 210 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT ACT_SITE 426 426 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 425 425 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 429 429 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 501 501 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT 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 //