ID   A0A1S6QJF8_9LACO        Unreviewed;       700 AA.
AC   A0A1S6QJF8;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   05-JUL-2017, entry version 3.
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
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}.
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DR   EMBL; CP018906; AQW21740.1; -; Genomic_DNA.
DR   RefSeq; WP_035168647.1; NZ_CP018906.1.
DR   Proteomes; UP000030361; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-HAMAP.
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:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0030163; P:protein catabolic process; IEA:UniProtKB-HAMAP.
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 cycle {ECO:0000313|EMBL:AQW21740.1};
KW   Cell division {ECO:0000313|EMBL:AQW21740.1};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01458};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030361};
KW   Hydrolase {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|HAMAP-Rule:MF_01458};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01458,
KW   ECO:0000256|RuleBase:RU003651};
KW   Protease {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       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   TRANSMEM    134    153       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   DOMAIN      222    361       AAA. {ECO:0000259|SMART:SM00382}.
FT   NP_BIND     230    237       ATP. {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   ACT_SITE    453    453       {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   METAL       452    452       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       456    456       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                MF_01458}.
FT   METAL       528    528       Zinc; catalytic. {ECO:0000256|HAMAP-Rule:
FT                                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
//