ID   C0ZCI2_BREBN            Unreviewed;       503 AA.
AC   C0ZCI2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Probable ATP-dependent zinc metallopeptidase {ECO:0000313|EMBL:BAH43491.1};
DE            EC=3.4.24.- {ECO:0000313|EMBL:BAH43491.1};
GN   OrderedLocusNames=BBR47_25140 {ECO:0000313|EMBL:BAH43491.1};
OS   Brevibacillus brevis (strain 47 / JCM 6285 / NBRC 100599).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=358681 {ECO:0000313|EMBL:BAH43491.1, ECO:0000313|Proteomes:UP000001877};
RN   [1] {ECO:0000313|EMBL:BAH43491.1, ECO:0000313|Proteomes:UP000001877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47 / JCM 6285 / NBRC 100599
RC   {ECO:0000313|Proteomes:UP000001877};
RA   Hosoyama A., Yamada R., Hongo Y., Terui Y., Ankai A., Masuyama W.,
RA   Sekiguchi M., Takeda T., Asano K., Ohji S., Ichikawa N., Narita S.,
RA   Aoki N., Miura H., Matsushita S., Sekigawa T., Yamagata H., Yoshikawa H.,
RA   Udaka S., Tanikawa S., Fujita N.;
RT   "Brevibacillus brevis strain 47, complete genome.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008955; BAH43491.1; -; Genomic_DNA.
DR   RefSeq; WP_012686196.1; NC_012491.1.
DR   AlphaFoldDB; C0ZCI2; -.
DR   STRING; 358681.BBR47_25140; -.
DR   KEGG; bbe:BBR47_25140; -.
DR   eggNOG; COG0465; Bacteria.
DR   HOGENOM; CLU_000688_16_2_9; -.
DR   Proteomes; UP000001877; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   PANTHER; PTHR23076:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 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|RuleBase:RU003651};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAH43491.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001877};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          105..249
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   503 AA;  55539 MW;  9E42CC8C9360012F CRC64;
     MRKEILIGVV PALLIFLVFL GVNITPFLVF GAVLGAIYFL VIRQQNGQGG NVALGGKRKA
     NKHELPKSDV QFADIGGQER AKKELKESLD FLVYKDKIEQ YGIRPIKGVL LTGPPGTGKT
     LMAKAAANYT NSAFVAASGS QFVEMYVGVG AQRVRELFQE AKALAEKNGQ DSAIIFIDEI
     DVVGGKRDGQ QQREYDQTLN QLLTEMDGVA TTDKPRILVM AATNRKDMLD AALLRPGRFD
     RHISVDLPDK PAREQILTIH TANKPLGEDV TLEKVAQETF GFSGAQLESV ANEAAIYAMR
     DRQDKITAKH FGYAVDKVML GEKVDRQASE EEKKRVALHE LGHAIVSESV RPGSVSQVTL
     SPRGKALGYV RQNPMEDRYL YTKEAMEKQI MVSLGGAVAE EIYYGGRSTG SKNDFEQALG
     MAQEIVQSGM SELGIVHLQY VDKNRIHDEV ERLLEGLLAE TRNLLRQFDS VFQTGLHTLL
     EAEVLQGDEF RALLSQTKEE VTV
//