ID C5QLJ5_9STAP Unreviewed; 709 AA. AC C5QLJ5; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 14-DEC-2022, entry version 72. 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; Staphylococcaceae; OC Staphylococcus. OX NCBI_TaxID=525378 {ECO:0000313|EMBL:EES42209.1, ECO:0000313|Proteomes:UP000003152}; RN [1] {ECO:0000313|EMBL:EES42209.1, ECO:0000313|Proteomes:UP000003152} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M23864:W1 {ECO:0000313|EMBL:EES42209.1, RC ECO:0000313|Proteomes:UP000003152}; RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L., RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A., RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R., RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R., RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P., RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y., RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L., RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.; RL Submitted (JAN-2009) 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: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 RefSeq; WP_002445687.1; NZ_GG696785.1. DR AlphaFoldDB; C5QLJ5; -. DR STRING; 525378.HMPREF0793_0101; -. DR MEROPS; M41.009; -. DR EnsemblBacteria; EES42209; EES42209; HMPREF0793_0101. DR GeneID; 58052122; -. DR eggNOG; COG0465; Bacteria. DR HOGENOM; CLU_000688_16_2_9; -. DR Proteomes; UP000003152; Unassembled WGS sequence. 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:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. 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; 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; FtsH protease domain-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR01241; FtsH_fam; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01458}; 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|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 7..25 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT TRANSMEM 110..133 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 197..336 FT /note="AAA" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 626..709 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..688 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 428 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 205..212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 427 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 431 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 503 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule: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 //