GenomeNet

Database: UniProt
Entry: Q3KFB4_PSEPF
LinkDB: Q3KFB4_PSEPF
Original site: Q3KFB4_PSEPF 
ID   Q3KFB4_PSEPF            Unreviewed;      1162 AA.
AC   Q3KFB4;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   OrderedLocusNames=Pfl01_1799 {ECO:0000313|EMBL:ABA73542.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA73542.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA73542.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA73542.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Required for chromosome condensation and partitioning.
CC       {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC       each terminus and a third globular domain forming a flexible hinge near
CC       the middle of the molecule. These domains are separated by coiled-coil
CC       structures. {ECO:0000256|HAMAP-Rule:MF_01894}.
CC   -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
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; CP000094; ABA73542.1; -; Genomic_DNA.
DR   RefSeq; WP_011333270.1; NC_007492.2.
DR   AlphaFoldDB; Q3KFB4; -.
DR   KEGG; pfo:Pfl01_1799; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_6; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR   CDD; cd03278; ABC_SMC_barmotin; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01894; Smc_prok; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR024704; SMC.
DR   InterPro; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
DR   InterPro; IPR011890; SMC_prok.
DR   NCBIfam; TIGR02168; SMC_prok_B; 1.
DR   PANTHER; PTHR43977; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   PANTHER; PTHR43977:SF1; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3; 1.
DR   Pfam; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_01894};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01894};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   DOMAIN          520..615
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          170..238
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          300..334
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          398..500
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          656..690
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          768..900
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
SQ   SEQUENCE   1162 AA;  131326 MW;  40BC26D1B4267637 CRC64;
     MRLKCIKLAG FKSFVDPTTV NFPSNMAAVV GPNGCGKSNI IDAVRWVMGE SSAKNLRGES
     MTDVIFNGST SRKPVSQASI ELVFDNSDGT LLGEWAAYAE ISIRRKVTRD SQTTYYLNGA
     KCRRRDITDI FLGTGLGPRS YSIIEQGMIS KLIESKPEDL RNFIEEAAGI SKYKERRRET
     ENRIRRTHEN LARLTDLREE LERQLERLHR QAEAAKKYQE YKAEERQLKA QLSALRWQDL
     NDQVSQRESI IGNQEISFEA LVAEQRNADA AIERLRDGHH DLSERFNLVQ GRFYSVGGDI
     ARVEQSIQHG QQRLRQLQDD LKEAERARLE TESHLGHDRT LLLTLGEELD QLTPEQEITN
     AAAEDAAAAL EDSETVMHGW QEQWDAFNLT AAEPRRQAEV QQSRIQQLET SMERLADRQK
     RLSEERALLS ADPEDAAIME LSEQLAESEA TLEDLQTSEA AQVEKLEQLR QELQQALTAQ
     QQAQGDLQRL NGRLASLEAL QQAALDPGTG TAEWLKEHNL AERPRLAEGL KVEAGWELAV
     ETVLGADLQA VLVDDFDGFD LSGFAQGDLR LLSPGNDGVR VAGSLLDKVE AQVDLSPWLA
     QVKPVDSLEQ ALALRGQLAA GQSLISRDGY WVGRHFLRVR RASEAESGML ARGQEIESLH
     AEREEREATV EAMEARLQTL RAQQRQQENG REHLRRLLQD EARQQGELKA QLSAGKAKAE
     QLNLRRTRLD EELVELAEQR ELEHENIGEA RIQLQEALDA MALDTEQREL LLAQRDSLRE
     RLDRVRQEAR QHKDHAHQLA VRLGSLRAQH DSTRQALERL EMQAERLTEK REQLSLNLEE
     GEAPLEELRL KLEELLDKRM SVDDELKTAQ IALEDADREL RDAEKRRTQA EQQSQLIRGQ
     LEQQRMEWQA LTVRRKALQD QLLEDGYDLH GVLNTLTAEA SERAAEEELE RIAARIQRLG
     AINLAAIDEY QQQSERKRYL DAQDADLVEA LETLENVIRK IDKETRNRFK DTFDQINGGL
     QALFPKVFGG GRAYLELTGE DLLDTGVTIM AQPPGKKNST IHLLSGGEKA LTALALVFAI
     FKLNPAPFCM LDEVDAPLDD ANVGRYARLV KEMSQTVQFI YITHNKIAME MADQLMGVTM
     HEPGCSRLVA VDVEEAMAMV DA
//
DBGET integrated database retrieval system