ID N9SJV7_9GAMM Unreviewed; 888 AA.
AC N9SJV7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=ClpV1 family type VI secretion ATPase {ECO:0000313|EMBL:ENX54891.1};
GN ORFNames=F901_02206 {ECO:0000313|EMBL:ENX54891.1};
OS Acinetobacter dispersus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=70348 {ECO:0000313|EMBL:ENX54891.1, ECO:0000313|Proteomes:UP000013195};
RN [1] {ECO:0000313|EMBL:ENX54891.1, ECO:0000313|Proteomes:UP000013195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIPH 1867 {ECO:0000313|EMBL:ENX54891.1,
RC ECO:0000313|Proteomes:UP000013195};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. NIPH 1867.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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:ENX54891.1}.
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DR EMBL; APRO01000007; ENX54891.1; -; Genomic_DNA.
DR RefSeq; WP_005211353.1; NZ_KB850086.1.
DR AlphaFoldDB; N9SJV7; -.
DR PATRIC; fig|1217702.3.peg.2133; -.
DR HOGENOM; CLU_005070_4_2_6; -.
DR Proteomes; UP000013195; 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; IPR028299; ClpA/B_CS2.
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; 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.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 8..154
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 468..527
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 888 AA; 98906 MW; E18B2C3A629B76D2 CRC64;
MSNLKVLITK LSPPTRTALE KSANFCINQL NYEIEIEHLF VELLNQNTAN DLHILLKKNN
ISPDALIADL KETISSLPKG NTRTPIFAKS IVRLFEQAWL LASAEQTPLI RSSHLLIALL
TAPDLQQIAF RASSLFELFP IDTMKHKFLD ICGKSSEQPQ TENTITSSAE PTDTPSTITA
AKTPALDQYT INLTEKAQNG GIDPVIGREF EIRLMLDILM RRRQNNPILT GEPGVGKTAV
VEGLALKIAQ GLVPEALKNV QLHSLDMGLL QAGASVKGEF ENRLKQVIKE VQASAHPIIL
FIDEAHTMIG AGGQAGQNDA ANLLKPALAR GELRTIAATT WAEYKQYFEK DAALSRRFQV
VKIEEPTEEV AIDMLRAMIP VMQNHFNLHI DDQAIITAVQ ASHRYISGRQ LPDKAVSVLD
TASARVALTQ NAQPVILDQF KAQQHNLKLE HQILTHEHQQ FPIHHQRLDD LNQQLTRLET
EIQETEIKWQ QELALVKQIQ QLNAQTETDH KAQIASLRAE LTQLQGQTPL VFERVNAQIV
NEIISDWTGI PVGNMVNDEI KQILTLEDKL GERVMGQDYA LAQLVQGIKT SKAKLEDPNK
PQGVFILIGP SGVGKTETAL ALANELYGGE QHLITINMSE YQEAHTVSSL KGAPPGYVGY
GQGGVLTEAV RRNPYSVVLL DEIEKAHSDV QELFYQVFDK GMLEDGEGRV IDFKNTTIIL
TSNTGSSAIM QACLNQPVEE WPHAEDLIEH LKPSLYKQFK PAFIGRMRIV PYFPLHDELL
VRIIKHKLGK IVARIEKQYA TKVQYSDDLI ELLLSRCTEV DSGARNVDNI LNSTVLPALA
TEILVALAEH KLPKLIVIDT KDDEITYQLD PVEKVTKKRS TKKTKAEV
//