ID   A0A7L5UFX0_9LACO        Unreviewed;       732 AA.
AC   A0A7L5UFX0;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   03-AUG-2022, 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=hflB {ECO:0000313|EMBL:QLL69345.1};
GN   Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN   ORFNames=GTO83_01590 {ECO:0000313|EMBL:QLL69345.1};
OS   Lactobacillus sp. 3B(2020).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus; unclassified Lactobacillus.
OX   NCBI_TaxID=2695882 {ECO:0000313|EMBL:QLL69345.1, ECO:0000313|Proteomes:UP000510624};
RN   [1] {ECO:0000313|EMBL:QLL69345.1, ECO:0000313|Proteomes:UP000510624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3B(2020) {ECO:0000313|Proteomes:UP000510624};
RA   Hassan H.M.;
RT   "Complete and circular genome sequences of six lactobacillus isolates from
RT   horses.";
RL   Submitted (JAN-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; CP047410; QLL69345.1; -; Genomic_DNA.
DR   Proteomes; UP000510624; 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: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   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; 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};
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   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        14..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   TRANSMEM        138..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          225..364
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          640..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        671..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         233..240
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         455
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         531
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   732 AA;  79985 MW;  C5F1D1A7EE099B9E CRC64;
     MNNNRKNNGF THNVLFYSVI FLCIMGIAYY FFGGRTHSGQ TKEVSQSEFI TELKDNKVKD
     FTVQPNGGVY KITGTYRKAQ SVSSSDKGGF SFASQASGTT KNFQSSVLQS EVTMGQLQKY
     ADHDKVKVTT KPEESNGFWA NLLTMILPLV IMIFFFYMMM GQAGQGGGGR GVMSFGKSKA
     KPADAKENKV RFSDVAGEEE EKQELVEVVE FLKNPKKFMK LGAKIPSGVL LEGPPGTGKT
     LLARAVAGEA GVPFFSISGS DFVEMFVGVG ASRVRDLFEQ AKKAAPAIIF IDEIDAVGRR
     RGNGMGGGHD EREQTLNQLL VEMDGFQGDE GVIVMAATNR ADVLDPALLR PGRFDRKILV
     GRPDVRGREA ILRVHAKNKP LASDVDLKEI AKQTPGFVGA DLANLLNEAA LLAARRNKTE
     IDAADVDEAE DRVIAGPAKR DRVISKQERR TVAYHEAGHT IVGLVLNDAR VVHKVTIVPR
     GRAGGYAIML PKEDQMLMSK KNAQEQIAGL MGGRAAEELI FKSQSSGASN DFEQATQIAR
     AMVTQYGMSE KIGPVELQSS GAVFTGQEFG QSPYSERTAA LIDEEVRRIL NEGHEEALHI
     IETHREQHRI IAEALLEYET LDEKQILSLY KTGKMPEKDV EVAEEEHRAQ TFEESKRELE
     RRENARATAT EEANDEAQTA DSVEQLANSA ADQPKPKQTS ASEEPKAPAT PSSETDESAS
     SSANSDSSSD ED
//