SMC_BACSU
ID SMC_BACSU Reviewed; 1186 AA.
AC P51834; O31735;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; Synonyms=ylqA;
GN OrderedLocusNames=BSU15940;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8654983; DOI=10.1016/0378-1119(96)00181-3;
RA Oguro A., Kakeshita H., Takamatsu H., Nakamura K., Yamane K.;
RT "The effect of Srb, a homologue of the mammalian SRP receptor alpha-
RT subunit, on Bacillus subtilis growth and protein translocation.";
RL Gene 172:17-24(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 236 AND 284.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1171-1186.
RC STRAIN=168;
RX PubMed=7584053; DOI=10.1093/dnares/2.2.95;
RA Oguro A., Kakeshita H., Honda K., Takamatsu H., Nakamura K., Yamane K.;
RT "srb: a Bacillus subtilis gene encoding a homologue of the alpha-subunit of
RT the mammalian signal recognition particle receptor.";
RL DNA Res. 2:95-100(1995).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=9573042; DOI=10.1101/gad.12.9.1254;
RA Britton R.A., Lin D.C., Grossman A.D.;
RT "Characterization of a prokaryotic SMC protein involved in chromosome
RT partitioning.";
RL Genes Dev. 12:1254-1259(1998).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9701812; DOI=10.1046/j.1365-2958.1998.00919.x;
RA Moriya S., Tsujikawa E., Hassan A.K., Asai K., Kodama T., Ogasawara N.;
RT "A Bacillus subtilis gene-encoding protein homologous to eukaryotic SMC
RT motor protein is necessary for chromosome partition.";
RL Mol. Microbiol. 29:179-187(1998).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894, ECO:0000269|PubMed:9573042,
CC ECO:0000269|PubMed:9701812}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- INTERACTION:
CC P51834; P35154: scpA; NbExp=20; IntAct=EBI-2121372, EBI-2121359;
CC P51834; P35155: scpB; NbExp=2; IntAct=EBI-2121372, EBI-2121445;
CC P51834; P51834: smc; NbExp=3; IntAct=EBI-2121372, EBI-2121372;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01894,
CC ECO:0000269|PubMed:9573042}. Note=Probably associated with the
CC nucleoid.
CC -!- DOMAIN: Contains large globular domains required for ATP hydrolysis at
CC each terminus and a third globular domain forming a flexible SMC hinge
CC near the middle of the molecule. These domains are separated by coiled-
CC coil structures. {ECO:0000255|HAMAP-Rule:MF_01894}.
CC -!- DISRUPTION PHENOTYPE: Mutants produce anucleate cells and show defects
CC in nucleoid structure and in chromosome partitioning.
CC {ECO:0000269|PubMed:9573042, ECO:0000269|PubMed:9701812}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP-
CC Rule:MF_01894}.
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; D64116; BAA10977.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13467.2; -; Genomic_DNA.
DR EMBL; D49781; BAA08615.1; -; Genomic_DNA.
DR PIR; G69708; G69708.
DR RefSeq; NP_389476.2; NC_000964.3.
DR RefSeq; WP_003232028.1; NZ_JNCM01000035.1.
DR PDB; 3ZGX; X-ray; 3.40 A; A/B=1-219, A/B=983-1186.
DR PDB; 5H66; X-ray; 1.82 A; A=1-199, B=1000-1186.
DR PDB; 5H67; X-ray; 2.07 A; A=1-199, B=1000-1186.
DR PDB; 5NMO; X-ray; 1.90 A; A/B=870-915, A/B=922-1011.
DR PDB; 5NNV; X-ray; 3.29 A; A/B/C/D=668-929.
DR PDB; 5XG3; X-ray; 3.50 A; A/B=1-219, A/B=224-259.
DR PDBsum; 3ZGX; -.
DR PDBsum; 5H66; -.
DR PDBsum; 5H67; -.
DR PDBsum; 5NMO; -.
DR PDBsum; 5NNV; -.
DR PDBsum; 5XG3; -.
DR AlphaFoldDB; P51834; -.
DR SMR; P51834; -.
DR DIP; DIP-52199N; -.
DR IntAct; P51834; 22.
DR STRING; 224308.BSU15940; -.
DR jPOST; P51834; -.
DR PaxDb; P51834; -.
DR PRIDE; P51834; -.
DR EnsemblBacteria; CAB13467; CAB13467; BSU_15940.
DR GeneID; 938085; -.
DR KEGG; bsu:BSU15940; -.
DR PATRIC; fig|224308.179.peg.1734; -.
DR eggNOG; COG1196; Bacteria.
DR InParanoid; P51834; -.
DR OMA; HNKIAME; -.
DR PhylomeDB; P51834; -.
DR BioCyc; BSUB:BSU15940-MON; -.
DR Proteomes; UP000001570; 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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
DR TIGRFAMs; TIGR02168; SMC_prok_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Cytoplasm; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1186
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000119028"
FT DOMAIN 519..637
FT /note="SMC hinge"
FT COILED 167..206
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 259..481
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 672..864
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 893..943
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 990..1029
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT CONFLICT 50
FT /note="E -> G (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="E -> G (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="K -> E (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="E -> G (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="E -> G (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="A -> P (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="A -> P (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="D -> G (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="E -> D (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..342
FT /note="KEELSKQ -> TRRAFEA (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="Q -> H (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="E -> K (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="I -> F (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 475
FT /note="A -> P (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="E -> D (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="E -> D (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="L -> V (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="A -> P (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 586..600
FT /note="QSRDAETAARHSSFL -> SKPLRGNSGPAFIISF (in Ref. 1;
FT BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 623..631
FT /note="TVLITEDLK -> NRSDYRGLKG (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="A -> S (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="S -> T (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="E -> G (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 694
FT /note="A -> S (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="K -> Q (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="L -> V (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT CONFLICT 738..740
FT /note="LQV -> PQF (in Ref. 1; BAA10977)"
FT /evidence="ECO:0000305"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 24..30
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 37..47
FT /evidence="ECO:0007829|PDB:5H66"
FT TURN 53..57
FT /evidence="ECO:0007829|PDB:5H67"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:5H67"
FT STRAND 76..85
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 168..196
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 236..247
FT /evidence="ECO:0007829|PDB:3ZGX"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:3ZGX"
FT HELIX 670..690
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 692..739
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 742..770
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 772..777
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 780..782
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 809..825
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 828..836
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 837..839
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 840..846
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 847..849
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 851..857
FT /evidence="ECO:0007829|PDB:5NNV"
FT TURN 858..864
FT /evidence="ECO:0007829|PDB:5NNV"
FT HELIX 870..915
FT /evidence="ECO:0007829|PDB:5NMO"
FT HELIX 922..949
FT /evidence="ECO:0007829|PDB:5NMO"
FT HELIX 953..959
FT /evidence="ECO:0007829|PDB:5NMO"
FT HELIX 966..981
FT /evidence="ECO:0007829|PDB:5NMO"
FT HELIX 1002..1052
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 1056..1062
FT /evidence="ECO:0007829|PDB:5H66"
FT TURN 1067..1069
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 1072..1077
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 1086..1088
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 1091..1108
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 1112..1118
FT /evidence="ECO:0007829|PDB:5H66"
FT TURN 1119..1122
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 1125..1127
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 1128..1138
FT /evidence="ECO:0007829|PDB:5H66"
FT TURN 1139..1141
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 1142..1147
FT /evidence="ECO:0007829|PDB:5H66"
FT HELIX 1151..1155
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 1158..1167
FT /evidence="ECO:0007829|PDB:5H66"
FT STRAND 1170..1177
FT /evidence="ECO:0007829|PDB:5H66"
SQ SEQUENCE 1186 AA; 135513 MW; ACC5D1A170453212 CRC64;
MFLKRLDVIG FKSFAERISV DFVKGVTAVV GPNGSGKSNI TDAIRWVLGE QSARSLRGGK
MEDIIFAGSD SRKRLNLAEV TLTLDNDDHF LPIDFHEVSV TRRVYRSGES EFLINNQPCR
LKDIIDLFMD SGLGKEAFSI ISQGKVEEIL SSKAEDRRSI FEEAAGVLKY KTRKKKAENK
LFETQDNLNR VEDILHELEG QVEPLKIQAS IAKDYLEKKK ELEHVEIALT AYDIEELHGK
WSTLKEKVQM AKEEELAESS AISAKEAKIE DTRDKIQALD ESVDELQQVL LVTSEELEKL
EGRKEVLKER KKNAVQNQEQ LEEAIVQFQQ KETVLKEELS KQEAVFETLQ AEVKQLRAQV
KEKQQALSLH NENVEEKIEQ LKSDYFELLN SQASIRNELQ LLDDQMSQSA VTLQRLADNN
EKHLQERHDI SARKAACETE FARIEQEIHS QVGAYRDMQT KYEQKKRQYE KNESALYQAY
QYVQQARSKK DMLETMQGDF SGFYQGVKEV LKAKERLGGI RGAVLELIST EQKYETAIEI
ALGASAQHVV TDDEQSARKA IQYLKQNSFG RATFLPLSVI RDRQLQSRDA ETAARHSSFL
GVASELVTFD PAYRSVIQNL LGTVLITEDL KGANELAKLL GHRYRIVTLE GDVVNPGGSM
TGGAVKKKNN SLLGRSRELE DVTKRLAEME EKTALLEQEV KTLKHSIQDM EKKLADLRET
GEGLRLKQQD VKGQLYELQV AEKNINTHLE LYDQEKSALS ESDEERKVRK RKLEEELSAV
SEKMKQLEED IDRLTKQKQT QSSTKESLSN ELTELKIAAA KKEQACKGEE DNLARLKKEL
TETELALKEA KEDLSFLTSE MSSSTSGEEK LEEAAKHKLN DKTKTIELIA LRRDQRIKLQ
HGLDTYEREL KEMKRLYKQK TTLLKDEEVK LGRMEVELDN LLQYLREEYS LSFEGAKEKY
QLETDPEEAR KRVKLIKLAI EELGTVNLGS IDEFERVNER YKFLSEQKED LTEAKNTLFQ
VIEEMDEEMT KRFNDTFVQI RSHFDQVFRS LFGGGRAELR LTDPNDLLHS GVEIIAQPPG
KKLQNLNLLS GGERALTAIA LLFSILKVRP VPFCVLDEVE AALDEANVFR FAQYLKKYSS
DTQFIVITHR KGTMEEADVL YGVTMQESGV SKVISVKLEE TKEFVQ
