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}.
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; 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
//