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Database: UniProt
Entry: D2ZY08_NEIMU
LinkDB: D2ZY08_NEIMU
Original site: D2ZY08_NEIMU 
ID   D2ZY08_NEIMU            Unreviewed;       883 AA.
AC   D2ZY08;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   SubName: Full=Type VI secretion ATPase, ClpV1 family {ECO:0000313|EMBL:EFC87962.1};
GN   Name=clpV {ECO:0000313|EMBL:EFC87962.1};
GN   ORFNames=NEIMUCOT_05515 {ECO:0000313|EMBL:EFC87962.1};
OS   Neisseria mucosa ATCC 25996.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=546266 {ECO:0000313|EMBL:EFC87962.1, ECO:0000313|Proteomes:UP000003344};
RN   [1] {ECO:0000313|EMBL:EFC87962.1, ECO:0000313|Proteomes:UP000003344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25996 {ECO:0000313|EMBL:EFC87962.1,
RC   ECO:0000313|Proteomes:UP000003344};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC       involved in the recovery of the cell from heat-induced damage, in
CC       cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675}.
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:EFC87962.1}.
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DR   EMBL; ACDX02000012; EFC87962.1; -; Genomic_DNA.
DR   RefSeq; WP_003743357.1; NZ_ACDX02000012.1.
DR   AlphaFoldDB; D2ZY08; -.
DR   STRING; 546266.NEIMUCOT_05515; -.
DR   GeneID; 61324367; -.
DR   eggNOG; COG0542; Bacteria.
DR   Proteomes; UP000003344; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017729; ATPase_T6SS_ClpV1.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR03345; VI_ClpV1; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF184; ATPASE WITH CHAPERONE ACTIVITY-RELATED; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          10..156
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          432..483
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   883 AA;  98037 MW;  2A27DEC1EEE37B4A CRC64;
     MSNISRSVLF GKLNTTLYKT LENAYTFCRL RENSYVELVH WLHSLLQTEK TDIFCLINSF
     NLDEARVRKD VLTAVEKLPA GSTAVIDFSE HIQTLVEQTW TYSSLKFGTD KIRTAHIFYT
     ILENKTLQSI VANISSEFLK IKPETLANNI VAITANSEEN LDVTQNALSS EPNATHKESA
     LTKYGSNLTE KAKNGEIDPL TGRDAEIRQM IDILMRRRQN NPILTGEAGV GKTAVVEALA
     LRLAAGDVPP GLKDVQLILL DIGLLKAGAS VSGEFESRLR AVMDEVESSP TPIVLFIDEI
     HTLIGAGGAA GTGDAANLLK PALARGKLRT IGATTWAEYK KYFEKDPALT RRFQVVQVDE
     PDENKAISML RALNASLEKH HNVIILDEAI QAAVKLSHRY IPARQLPDKA VGLIDTACAR
     VAVSQHAVPG SIEFLRKKSE ALKLEQANLE REKKLSFDSE TRITNIGKEL TEVEGRLKKL
     EDRWKSETDL VTELLDVREQ IMHAEEGTAE KETKQLYTRQ KELVNKLKKL QGIQPLVMPL
     VDSRTVADVV ADWTGIPVGK MMKDEVEAVL QLADTLNKRI IGQRHGLDAI SRRIQTSRAN
     LDNPNKPIGV FMLAGPSGVG KTETALALAD TLYGGEQNVI TINMSEYQEA HTVSTLKGAP
     PGYVGYGEGG VLTEAVRRKP YSVILLDEVE KAHPDVHEIF FQVFDKGWME DGEGRYIDFK
     NTIIILTTNV GTDLIMDMCD DPEMLPTPEG LTKALRAPML KTFPAALLGR MQVIPYYPLS
     DDMLSKIVEL QLGRIVDRIK DNHGIDLHYT PEVLKLITSR CTEVESGGRM IDAILTNTVL
     PQISRELLTS ATQGKQILSI NINASNHDFT YQYKYKPRKK NAL
//
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