ID K9VYW0_9CYAN Unreviewed; 641 AA.
AC K9VYW0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=Cri9333_2272 {ECO:0000313|EMBL:AFZ13141.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ13141.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ13141.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ13141.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) 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: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01458}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01458}; Stromal 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}.
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DR EMBL; CP003620; AFZ13141.1; -; Genomic_DNA.
DR AlphaFoldDB; K9VYW0; -.
DR STRING; 1173022.Cri9333_2272; -.
DR MEROPS; M41.017; -.
DR KEGG; cep:Cri9333_2272; -.
DR PATRIC; fig|1173022.3.peg.2458; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_1_3; -.
DR OrthoDB; 548807at2; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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; 3.30.720.210; -; 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; IPR011546; Pept_M41_FtsH_extracell.
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; PF06480; FtsH_ext; 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 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:UP000010472};
KW Thylakoid {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 136..158
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT DOMAIN 221..360
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT ACT_SITE 451
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 229..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
FT BINDING 528
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01458"
SQ SEQUENCE 641 AA; 70405 MW; BEB2689232062476 CRC64;
MNNSSWNKAS LGRNTPIGFS FLRPTKQMAS VPKAPRTIWR LAVSWMILQG VFLGTPAIAK
PDQDALSYTQ LLQKIEAGEV SKLEIDPATQ VAKVTLKQKP TETEQIRLFE QNPELIEKIR
KNNVDFEVQT STDNSVALGL AANLFFIFLV LAAVTMLFRR SSNASGQALN FGKSRARFQM
EAKTGVLFDD VAGIAEAKEE LQEVVTFLKQ PERFTAVGAK IPKGVLLVGP PGTGKTLLAK
AIAGEAGVPF FSISGSEFVE MFVGVGASRV RDLFKKAKEN APCLVFIDEI DAVGRQRGTG
IGGGNDEREQ TLNQLLTEMD GFEGNTGIII IAATNRPDVL DSALLRPGRF DRQVMVDAPD
LKGRLSILEV HARNKKIDPE VSLEAIARRT PGFTGADLAN LLNEAAILTA RRRKDAVTML
EIDDAIDRVV AGMERTPLVD SKNKRLIAYH EIGHAIIGTL LKHHDPVQKV TLIPRGQAQG
LTWFTPGEEQ GLISRGQLLA RISGALGGRA AEQIIFGDAE VTTGAGADLE YISSLARQMV
TRFGMSTLGP VSLENPNSEV FLGRDFMSRS EYSEEISSQI DAQVRAIIDY CYKEALQLIR
ENRHLVDRLV DILLDKETIE GEEFRKIVTE YNQRVEKHLA V
//