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Database: UniProt
Entry: A0A1V4IMC3_9CLOT
LinkDB: A0A1V4IMC3_9CLOT
Original site: A0A1V4IMC3_9CLOT 
ID   A0A1V4IMC3_9CLOT        Unreviewed;       602 AA.
AC   A0A1V4IMC3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 29.
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_1 {ECO:0000313|EMBL:OPJ61066.1};
GN   Synonyms=ftsH {ECO:0000256|HAMAP-Rule:MF_01458};
GN   ORFNames=CLORY_24610 {ECO:0000313|EMBL:OPJ61066.1};
OS   Clostridium oryzae.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1450648 {ECO:0000313|EMBL:OPJ61066.1, ECO:0000313|Proteomes:UP000190080};
RN   [1] {ECO:0000313|EMBL:OPJ61066.1, ECO:0000313|Proteomes:UP000190080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28571 {ECO:0000313|EMBL:OPJ61066.1,
RC   ECO:0000313|Proteomes:UP000190080};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium oryzae DSM 28571.";
RL   Submitted (MAR-2017) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01458}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ61066.1}.
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DR   EMBL; MZGV01000025; OPJ61066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4IMC3; -.
DR   STRING; 1450648.CLORY_24610; -.
DR   OrthoDB; 9809379at2; -.
DR   Proteomes; UP000190080; Unassembled WGS sequence.
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   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 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   NCBIfam; TIGR01241; FtsH_fam; 1.
DR   PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR   PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
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; FtsH protease domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|ARBA:ARBA00023136, 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:UP000190080};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01458};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01458}; Zinc {ECO:0000256|HAMAP-Rule:MF_01458}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..602
FT                   /note="ATP-dependent zinc metalloprotease FtsH"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039187638"
FT   TRANSMEM        104..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   DOMAIN          191..330
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         199..206
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         421
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         425
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT   BINDING         497
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ   SEQUENCE   602 AA;  66182 MW;  95D02B72B501E763 CRC64;
     MKKFSTATAW VLLLIMTVVA ALVLVHGTNG ANTITADQFE KYWNNDKVKQ IQVSSNLFSV
     EGSLTDGRQF QVDVPYERVL QIMHKHPNNG SVVEKYEKAT TIPLWVQSIP NILLIVMLIA
     FWFLFMQQSQ GGGGNRGVMN FGKSRAKMAN PDKKKVTFKD VAGADEEKAE LAEIVDFLKQ
     PKKYTDMGAR IPKGLLLVGP PGTGKTLLAK AISGEAGVPF FSISGSDFVE MFVGVGASRV
     RDLFEQAKKQ APCIVFIDEI DAVGRQRGAG LGGGHDEREQ TLNQLLVEMD GFGINEGIII
     IAATNRPDIL DHALLRPGRF DRQIFVGSPD VRGREEILKV HSKNKPISSD VKLDVLAKTT
     PGFTGADLEN LMNEAALLAV RNNKKVIEME ELEEAMTRVV AGPEKKSRVM SEHDRKLTAY
     HEAGHAVVMK LLPDHDPVHQ ISIIPRGMAG GFTMPLPNED RSYTSKSHLE AEMVSLLGGR
     VAEKLIIGDI STGAKSDIDK ATSIARKMIM EYGMSDVIGP ISMGEDREEV FLGRDLGRNR
     NFSEEVAATI DREIKSLIDD AYNKAESLLT ENINKLHAVA QALLEKEKLE GSEFDEIFQA
     AV
//
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