ID   A0A1S6QJF8_9LACO        Unreviewed;       700 AA.
AC   A0A1S6QJF8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   02-DEC-2020, entry version 17.
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=PL11_007305 {ECO:0000313|EMBL:AQW21740.1};
OS   Lactobacillus curieae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1138822 {ECO:0000313|EMBL:AQW21740.1, ECO:0000313|Proteomes:UP000030361};
RN   [1] {ECO:0000313|EMBL:AQW21740.1, ECO:0000313|Proteomes:UP000030361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC M 2011381 {ECO:0000313|EMBL:AQW21740.1,
RC   ECO:0000313|Proteomes:UP000030361};
RX   PubMed=26021929;
RA   Wang Y., Wang Y., Lang C., Wei D., Xu P., Xie J.;
RT   "Genome Sequence of Lactobacillus curieae CCTCC M 2011381T, a Novel
RT   Producer of Gamma-aminobutyric Acid.";
RL   Genome Announc. 3:0-0(2015).
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; CP018906; AQW21740.1; -; Genomic_DNA.
DR   RefSeq; WP_035168647.1; NZ_CP018906.1.
DR   STRING; 1138822.PL11_09795; -.
DR   KEGG; lcu:PL11_007305; -.
DR   eggNOG; COG0465; Bacteria.
DR   OrthoDB; 190468at2; -.
DR   Proteomes; UP000030361; 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: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: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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01458, ECO:0000256|RuleBase:RU003651};
KW   Cell cycle {ECO:0000313|EMBL:AQW21740.1};
KW   Cell division {ECO:0000313|EMBL:AQW21740.1};
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:UP000030361};
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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   TRANSMEM        134..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          222..361
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   NP_BIND         230..237
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   REGION          624..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..640
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..700
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        453
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           452
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           456
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   METAL           528
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   700 AA;  76944 MW;  A20B431C8BB02F45 CRC64;
     MNSNKNGLFR SSLFYIVMFL LVMGVIYFFS GSNTNTQSQE IRSSQFVQNL KDDKIKNFSI
     QPSGGVYKVT GEYRQAQKVK EQTGLLIGGS TQTKDVSKFS TTVLENNTSV AEITKAAQDN
     KVKMNAKPEE SSGFWVNLLV YVLPLVIFIW FFYMMMGKAG GQGGGNGRVM NFGKSKAKPA
     DSKQNKVRFS DVAGEEEEKQ ELVEVVEFLK DPRKFTSLGA KIPHGVLLEG PPGTGKTLLA
     KAVAGEAGVP FYSISGSDFV EMFVGVGASR VRDLFEQAKK AAPAIIFIDE IDAVGRKRGA
     GMGGGHDERE QTLNQLLVEM DGFEGNEGVI VIAATNRSDV LDPALTRPGR FDRKILVGRP
     DVNGREAILK VHSKNKPLSS NVDLHEIAKQ TPGFVGADLA NLLNEAALLA ARRNKADIDA
     SDVDEAEDRV IAGPAKRNRV ISKHERETVA YHEAGHTIVG LVLNDARVVH KVTIVPRGRA
     GGYAIMLPKE DQQLMSKKDA QEQIAGLMGG RAAEEIIFNS ESSGASNDFE QATNIARAMV
     TQYGMSDKLG RVQLENPSEE AYGPRYSQET AASIDDEVRR FTDEGHAEAT RIIEEHRDQH
     RIIAEALLKY ETLDEKQILS LYNTGKMPED PSTSDFPSER ASTFEEAKRE LERKEAERQA
     SIEKGKDNSD ETDTSSTDPQ PDDVKPDNDS QNNHQNNDDE
//