ID   A0A0B4XTU8_9GAMM        Unreviewed;       644 AA.
AC   A0A0B4XTU8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   12-AUG-2020, entry version 22.
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=S7S_16525 {ECO:0000313|EMBL:AJD49717.1};
OS   Alcanivorax pacificus W11-5.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD49717.1, ECO:0000313|Proteomes:UP000006764};
RN   [1] {ECO:0000313|EMBL:AJD49717.1, ECO:0000313|Proteomes:UP000006764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W11-5 {ECO:0000313|EMBL:AJD49717.1,
RC   ECO:0000313|Proteomes:UP000006764};
RX   PubMed=23209202; DOI=10.1128/JB.01845-12;
RA   Lai Q., Shao Z.;
RT   "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT   type strain W11-5, isolated from deep sea sediment.";
RL   J. Bacteriol. 194:6936-6936(2012).
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}.
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DR   EMBL; CP004387; AJD49717.1; -; Genomic_DNA.
DR   MEROPS; M41.001; -.
DR   EnsemblBacteria; AJD49717; AJD49717; S7S_16525.
DR   KEGG; apac:S7S_16525; -.
DR   HOGENOM; CLU_000688_16_0_6; -.
DR   KO; K03798; -.
DR   Proteomes; UP000006764; Chromosome.
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-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.58.760; -; 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; SSF140990; 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}; Cell cycle {ECO:0000313|EMBL:AJD49717.1};
KW   Cell division {ECO:0000313|EMBL:AJD49717.1};
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:UP000006764};
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        101..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          189..328
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NP_BIND         197..204
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   REGION          602..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        420
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           419
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           423
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           497
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   644 AA;  70524 MW;  A92D68570C7A095F CRC64;
     MNDMTKNIVL WLVIAGVLYV VAQGISHEPT VQTVDYSEFI KRVENGGVAR VEIQDYRIRG
     EDRQGKLFET VKPPVADLDL MPTLIQNNVR VEGKEPERQG FMTQLFLSVL PILLILAIFI
     FFMRQMQGGG KGGGGPMTFG KSKARLLSED QIKTTFADVA GVEEAKEEVQ ELVEFLRDPA
     KFQRLGGRIP RGVLMVGSPG TGKTLLAKAI AGEARVPFFS ISGSDFVEMF VGVGASRVRD
     MFEQAKKHAP CIIFIDEIDA VGRSRGAGLG GGHDEREQTL NQLLVEMDGF GANDGIIVIA
     ATNRPDVLDA ALLRPGRFDR QVVVPLPDVR GREQIIKVHM RNVPVADDVN PSLIARGTPG
     FSGADLANLV NEAALFAARG NKRLVSMEEF ERAKDKILMG AERRSMVMNE KEKLNTAYHE
     AGHAIIGRVV PEHDPVYKVS IIPRGRALGV TMYLPTEDKY SQSKRALESM ICSLFGGRIA
     EEMINGFDGV TTGASNDIER ATKLARAMVT KWGLSEKLGP LAYEEEEGEV FLGKTMSQTK
     HVSEEIAQEI DREVRAIIDD CYGRAKQILE DNRDKLETMA QALMQYETID ADQIEDIMNG
     RQVRPPKDWQ DPGPGTGSPS TGAAPDGEPT PKGEGPIGGP ANTH
//