ID A0A0Q0HKA2_9GAMM Unreviewed; 649 AA. AC A0A0Q0HKA2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 7. 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|EMBL:KPZ74040.1, ECO:0000313|Proteomes:UP000050391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1-26 {ECO:0000313|EMBL:KPZ74040.1, RC ECO:0000313|Proteomes:UP000050391}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) 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: Lacks conserved residue(s) required for the propagation CC of feature annotation. {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: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 EnsemblBacteria; KPZ74040; KPZ74040; AN394_01034. DR Proteomes; UP000050391; 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: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; 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 ECO:0000256|RuleBase:RU003651}; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458}; KW Complete proteome {ECO:0000313|Proteomes:UP000050391}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000313|EMBL:KPZ74040.1}; 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 ECO:0000313|EMBL:KPZ74040.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000256|RuleBase:RU003651}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01458, KW ECO:0000313|EMBL:KPZ74040.1}; 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 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT DOMAIN 189 328 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 197 204 ATP. {ECO:0000256|HAMAP-Rule:MF_01458}. FT ACT_SITE 420 420 {ECO:0000256|HAMAP-Rule:MF_01458}. FT METAL 419 419 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 423 423 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT MF_01458}. FT METAL 497 497 Zinc; catalytic. {ECO:0000256|HAMAP-Rule: FT 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 //