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
//