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Database: UniProt
Entry: Q6MNS9_BDEBA
LinkDB: Q6MNS9_BDEBA
Original site: Q6MNS9_BDEBA 
ID   Q6MNS9_BDEBA            Unreviewed;      1195 AA.
AC   Q6MNS9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN   ECO:0000313|EMBL:CAE79072.1};
GN   OrderedLocusNames=Bd1158 {ECO:0000313|EMBL:CAE79072.1};
OS   Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS   HD100).
OC   Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC   Pseudobdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=264462 {ECO:0000313|EMBL:CAE79072.1, ECO:0000313|Proteomes:UP000008080};
RN   [1] {ECO:0000313|EMBL:CAE79072.1, ECO:0000313|Proteomes:UP000008080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100
RC   {ECO:0000313|Proteomes:UP000008080};
RX   PubMed=14752164; DOI=10.1126/science.1093027;
RA   Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA   Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA   Schuster S.C.;
RT   "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT   genomic perspective.";
RL   Science 303:689-692(2004).
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}.
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DR   EMBL; BX842649; CAE79072.1; -; Genomic_DNA.
DR   RefSeq; WP_011163674.1; NC_005363.1.
DR   AlphaFoldDB; Q6MNS9; -.
DR   STRING; 264462.Bd1158; -.
DR   KEGG; bba:Bd1158; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_7; -.
DR   Proteomes; UP000008080; 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; 1.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 6.10.140.1720; -; 1.
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; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008080}.
FT   DOMAIN          534..650
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          191..362
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          412..446
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          698..809
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          845..921
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          1007..1041
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   1195 AA;  135433 MW;  CAF5ACAE74826B7C CRC64;
     MRIKKIELIG FKSFKDRTVI HFDAGITGIV GPNGCGKSNI VDALMWVMGD QSAKDLRASQ
     MTDVIFGGAE GYAPLGMCEV SLTLENDGGP FPAKYIKHSE IMVTRRLHRN GEGEYFINKE
     PARLKDLQEI FMDTGAGSKG FSIIAQGMIG KIITAKPEDR RMLIEEAAGI TKFKARKKES
     QRKLVATDQN LVRLQDIIGE LKRQIDSLQR QAQRAERYRN IKNQIEDLDL WLSTAQYVEL
     KRAADEAQAI FNEAQSMEVE GETNLSTLQG QLEVLKLQIL EKEKAVEEQQ TEYFTKQSTV
     QKKEMEIQEL RFEIEQARRN EQMTGTILQE QQARKELLAR DKAALDEQVT ELKEESESLS
     AAFAEKNEIF QNFNSRIGTV DEDLTTKRRE LFAVGQTESS LDARVNSLSS QIADLTDRQD
     NEQQVLNELR EKQVEFENRR KKVITELDKE RQMQLDLASD VDSFEANKKI LQDSVATKKA
     EVDSFKDSLN EVASRLYGLE NLQNNFEGFQ EGVKQVMLWQ KTRTQEMMAD GSVVSHFQPV
     SEVVEVPAEY EVAMEAALGS RLQMLLSSDA NIAVDAVSHL KENKSGRSSF MAADGQGLTF
     NRAEAPMGQD GVQAILKDVV QAADKFKNTV TYMLDGVAIV DSIRTALNLR PRYEGWTFVT
     LDGDTLTADG VLTGGSSESA DSGMLKRRRE IKELSEKKDE FAGKLQLAQM ALKKTEEQLA
     NVLNDFEGAQ KRKIDQEIKV AELRKDAERA ENEVQNALAA VERQEREVKK LTEQLEVQEQ
     KLEELNEALI EARERKVLLE TEVETLNSEM NSVRLGFDGL QAEVTDLQVK SASKTQEYTG
     VLRQLEMVTK SLTDLEAQLA RMSEEAEGYN SQMTDTQVTL EEKKIEFERL LDEVETLKLQ
     AARAKDEYEV MSESIRAIED EASASQRARN ERQHKMNDSQ LKLEQAKMKE QYLIDQVRER
     YMLNLPDVVE KYVNREGDFL EADAQLKDLR EKLAKIGEVN LSAIEEYEET AQRYEFLTKQ
     HADLTEAKDQ LRKVIERINK ICSKRFKETF ELVNDRFTRV FPVLFGGGEA WLELVEETEK
     NEAGIEIIAR PPGKKTQNVS LMSGGEKALT AVALVFSIFL VKPSPWCLLD EVDAPLDDAN
     VFRFNDLVRE MAKRSQIIVV THNKHTMEVA GKLYGVTMQE RGVSTMVSVS IQDIK
//
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