ID C5QLJ5_9STAP Unreviewed; 709 AA. AC C5QLJ5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 26-NOV-2014, entry version 32. 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 Synonyms=hflB {ECO:0000313|EMBL:EES42209.1}; GN ORFNames=HMPREF0793_0101 {ECO:0000313|EMBL:EES42209.1}; OS Staphylococcus caprae M23864:W1. OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES42209.1}; RN [1] {ECO:0000313|EMBL:EES42209.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES42209.1}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., RA Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., RA Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y., RA Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L., RA Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F., RA Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M., RA Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S., RA Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J., RA Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J., RA Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D., RA Worley K., Gibbs R.; RL Submitted (JAN-2009) 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 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: 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:EES42209.1}. 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; ACJB01000005; EES42209.1; -; Genomic_DNA. DR ProteinModelPortal; C5QLJ5; -. DR MEROPS; M41.009; -. DR EnsemblBacteria; EES42209; EES42209; HMPREF0793_0101. DR PATRIC; 31399242; VBIStaEpi14170_2476. 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:0030163; P:protein catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. 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 Pfam; PF00004; AAA; 1. DR Pfam; PF06480; FtsH_ext; 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 Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000313|EMBL:EES42209.1}; 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 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 TOPO_DOM 1 6 Cytoplasmic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT TRANSMEM 7 27 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT TOPO_DOM 28 110 Extracellular. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT TRANSMEM 111 131 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT TOPO_DOM 132 709 Cytoplasmic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT NP_BIND 205 212 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT ACT_SITE 428 428 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 427 427 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 431 431 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 503 503 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. SQ SEQUENCE 709 AA; 78826 MW; 6379C07DF8724845 CRC64; MQKAFRNVLV IAIIGVIIFG VFSFLNGNGN MPKQLTYTQF VNKLDKGDLK SLEIQPEQNV YMVSGKTKSG DDYSSTVLYN NEKDLQKITD TAKKQDGLKF TVKEEEKQSV FVSILTTLIP VLIIALLFIF FLSQAQGGGG GGRMMNFGKS KAKMYDSNKR RVRFSDVAGA DEEKQELIEI VDFLKDNKKF KQMGSRIPKG VLLVGPPGTG KTLLARAVAG EAGAPFFSIS GSDFVEMFVG VGASRVRDLF ENAKKNAPCI IFIDEIDAVG RQRGAGVGGG HDEREQTLNQ LLVEMDGFGE NEGIIMIAAT NRPDILDPAL LRPGRFDRQI QVGRPDVKGR EAILHVHARN KPLDETVDLK AISQRTPGFS GADLENLLNE ASLIAAREGK NKIDMRDIEE ATDRVIAGPA KKSRVISEKE RNIVAHHEAG HTIIGMVLDE AEVVHKVTIV PRGQAGGYAM MLPKQDRFLM TEPELLDKIC GLLGGRVSED INFGEVSTGA SNDFERATQI ARSMVTEYGM SKKLGPLQFS SSSGGQVFLG KDMQGEPNYS GQIAYEIDKE VQRIVKEQYE RCKQILLEHE EQLKLIAKTL LTEETLVAEQ IRSLFNEGKL PEVDYDAAKV VKDEDTDYSD GKYGKSYDDI RKEQLEEGHK EEEQDRKEDR EIDKERRQQE DRDRSGSESD HDSDSEATGH EQSPNIDKPY DPSNPDNRH //