ID   G7GEB7_9GAMM            Unreviewed;       889 AA.
AC   G7GEB7;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Putative type VI secretion system family protein {ECO:0000313|EMBL:GAB01942.1};
GN   ORFNames=ACT4_023_01180 {ECO:0000313|EMBL:GAB01942.1};
OS   Acinetobacter sp. NBRC 100985.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1071390 {ECO:0000313|EMBL:GAB01942.1, ECO:0000313|Proteomes:UP000012044};
RN   [1] {ECO:0000313|EMBL:GAB01942.1, ECO:0000313|Proteomes:UP000012044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100985 {ECO:0000313|EMBL:GAB01942.1,
RC   ECO:0000313|Proteomes:UP000012044};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Acinetobacter sp. NBRC 100985.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {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:GAB01942.1}.
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DR   EMBL; BAEB01000023; GAB01942.1; -; Genomic_DNA.
DR   RefSeq; WP_007481650.1; NZ_BAEB01000023.1.
DR   AlphaFoldDB; G7GEB7; -.
DR   Proteomes; UP000012044; 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; 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; 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}.
FT   DOMAIN          223..368
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          602..746
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          776..868
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          437..528
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   889 AA;  99293 MW;  DBC6BC1016B52274 CRC64;
     MSNLKVLITK LSQPTRSALE KSANYCINQL NYEIEIEHLF VELLNQKDPN DLLILLKKNN
     ISYEALINDL KETILSLPKG NTRTPIFAKS IVKLFEQAWL LASAEQTPII RSGHLLVALL
     TAPDLQQIAA RASSLFELFP IDTMKHKFLD ICEQSSEQTQ IENSLSIDGQ QNKSQNAPIP
     VKTPALDQYT INLTEKAQKG LIDPVIGREF EIRLMLDILM RRRQNNPILT GEPGVGKTAV
     VEGLALKIAQ GLVPEALKNV HIHVLDMGLL QAGASVKGEF ENRLKQVIQE VQASTHPIIL
     FIDEAHTLIG AGGQAGQNDA ANLLKPALAR GELRTIAATT WAEYKQYFEK DAALSRRFQV
     VKVEEPTEEV AIDMLRAMIP VMQNHFNLHI DDQAIITAVQ ASHRYISGRQ LPDKAVSVLD
     TAAARVALTQ NAQPVLLDQL KAQQHNLNLE QQILIQEHQH FPIHHERLES LKQQLATLDQ
     DIQATEEKWQ QELKLVQEIN QLNTQSEDES AHSKIEALRT ELEQLQGQAP LVFERVNARI
     INEIISDWTG IPVGNMVNDE IKQILTLEDK LAERVMGQDY ALSQLVQGIK TSKAKLEDPN
     KPQGVFLLVG PSGVGKTETA LALANELYGG EQHLITINMS EYQEAHTVSS LKGAPPGYVG
     YGQGGVLTEA VRRNPYSVVL LDEIEKAHSD VQELFYQVFD KGMLEDGEGR IIDFKNTTIL
     LTSNTGSSAI MQACLNQPVE DWPNAEDLIE HLKPSLYKQF KPAFIGRMRI VPYFPLHDDL
     LVRIIKHKLG KIIQRIENQY ATAVEYSDDL VELLLSRCTE VDSGARNVDN ILNSSVLPSL
     ATEILVALAE HKLPKRIVID IKDDDISYQL DPAEKVTKMR TSKKTKADV
//