ID A0A0Q0HKA2_9GAMM Unreviewed; 649 AA. AC A0A0Q0HKA2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 22-FEB-2023, entry version 27. 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 ECO:0000313|EMBL:KPZ74040.1}; GN ORFNames=AN394_01034 {ECO:0000313|EMBL:KPZ74040.1}; OS Pseudoalteromonas sp. P1-26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1723759 {ECO:0000313|EMBL:KPZ74040.1, ECO:0000313|Proteomes:UP000050391}; RN [1] {ECO:0000313|Proteomes:UP000050391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1-26 {ECO:0000313|Proteomes:UP000050391}; RA Klassen J.L., Wolf T., Rischer M., Guo H., Shelest E., Clardy J., RA Beemelmanns C.; RL Submitted (SEP-2015) 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:KPZ74040.1}. 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; LKDX01000006; KPZ74040.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0Q0HKA2; -. DR EnsemblBacteria; KPZ74040; KPZ74040; AN394_01034. DR PATRIC; fig|1723759.3.peg.1043; -. DR Proteomes; UP000050391; 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 CDD; cd00009; AAA; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.30.720.210; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 1.20.58.760; Peptidase M41; 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 PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1. DR PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1. 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|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; 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:UP000050391}; 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 103..124 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT DOMAIN 189..328 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT REGION 599..649 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 600..649 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 420 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 197..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 419 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 423 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" FT BINDING 497 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458" SQ SEQUENCE 649 AA; 71205 MW; 8F4D11E031E08362 CRC64; MSDMAKNLIL WLVIAVVLMS VFQSFNGGDQ ADRQTSYTQF VSDARSGAIQ EVSIESTTGT ITGTKTNGER FQTIMPMYDK DILNDLLKSN VNVKGVKPEE QSFLASILIS WFPMLLLIGV WIFFMRQMQG GGGKGAMSFG KSKARLMSED QVKTTFADVA GCDEAKEDVT ELVDFLRDPS KFQKLGGSIP KGVLMVGPPG TGKTLLAKAV AGEAKVPFFT ISGSDFVEMF VGVGASRVRD MFEQAKKAAP CIIFIDEIDA VGRKRGAGMG GGHDEREQTL NQMLVEMDGF EGNEGIIVIA ATNRPDVLDP ALLRPGRFDR QVVVGLPDIR GREQILKVHM RKVPLGDNVE AAVIARGTPG FSGADLANLV NEAALYAARG NKRVVSMAEF DAAKDKIMMG AERKTMVMSE QEKEMTAYHE AGHAIVGRMV PEHDPVYKVS IIPRGRALGV TMYLPEQDRV SHSKELLESM ISSLYGGRIA EALIYGEDKV TTGASNDIER ATDIARKMVT QWGLSEKLGP LLYAEDQNEM YMGGGGSRAM SMSDETAKVI DTEVRLFSDR NYQRAEQILK DNIDILHAMK DALMKYETID AGQIDDLMAR QPVREPRDVH DRRSDDKKPA PSAAKVVEND TKEPEESSET KTNVDDKAE //