ID   A0A0Q0HKA2_9GAMM        Unreviewed;       649 AA.
AC   A0A0Q0HKA2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   18-JAN-2017, entry version 6.
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}.
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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   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   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
//