ID   A0A7T6Z7T9_9BACI        Unreviewed;       690 AA.
AC   A0A7T6Z7T9;
DT   29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 1.
DT   19-JAN-2022, entry version 2.
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=HUG20_00525 {ECO:0000313|EMBL:QQK78555.1};
OS   Salicibibacter cibi.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Salicibibacter.
OX   NCBI_TaxID=2743001 {ECO:0000313|EMBL:QQK78555.1, ECO:0000313|Proteomes:UP000595349};
RN   [1] {ECO:0000313|EMBL:QQK78555.1, ECO:0000313|Proteomes:UP000595349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NKC21-4 {ECO:0000313|EMBL:QQK78555.1,
RC   ECO:0000313|Proteomes:UP000595349};
RA   Oh Y.J.;
RT   "Genomic analysis of Salicibibacter sp. NKC21-4.";
RL   Submitted (JUN-2020) 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}.
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DR   EMBL; CP054706; QQK78555.1; -; Genomic_DNA.
DR   Proteomes; UP000595349; Chromosome.
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; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01458}; Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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   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..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   TRANSMEM        117..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          202..341
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NP_BIND         210..217
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   REGION          615..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          578..598
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        632..668
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        433
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           432
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           436
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           508
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   690 AA;  76489 MW;  FB88756CDCBE4CA0 CRC64;
     MNRTVRYTFF WLFVLLILIG IVQLFTDDPV EDEMMNTDEF MQALEQDEIA SMTVQPEMEV
     YLIEGEMVNG GEEDEANEFT AHILRSPEVT DMLLDAMETN ESLTAVDTEP GEEPGGWLQF
     LVAVIPFIII FILFFFLLSQ MQGGGNKMMN FGKSKAKMQQ ESDKKKARFK DVAGAEEEKQ
     ELVEIVDFLK DPRKFANIGA RIPKGVLLVG PPGTGKTLLG RAVAGEAGVP FFSISGSDFV
     EMFVGVGASR VRDLFNNAKN NAPCIIFIDE LDAVGRQRGA GVGGGHDERE QTLNQLLVEM
     DGFEGNEGII IIAATNRSDV LDPALLRPGR FDRQITVGLP DVRGREDVLK VHVREKPIDD
     DVELGAIAQR TPGFSGAELE NLLNEAALVA ARSNSVKIKM VHIEEAIDRV IAGPAKKTRV
     ISEKEKNIVA HHEAGHTVVG VKLQNADAVH KVTIVPRGQA GGYAMMLPKE DRYFMTKPEL
     LDKIVGLLGG RVSEDIIFGE ASTGAHNDFQ RATAIARKMV MEYGMSEKLG PLQFGSTGGG
     QVFLGRDIQN EQNYSDAIAH EIDKEVQKII KDSYERCRQI LTENKDKLEL VAQNLLELET
     LDAEQIYSLV EEGKLPEGHH SNQTQEDALK NSGDVDPVDD ENVKVNIGSQ EEEQPETKND
     QSKANEETEE QDQTEEQDNE EKQEDDNRRS
//