SMC_CAUVN
ID SMC_CAUVN Reviewed; 1147 AA.
AC B8GZ28;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=CCNA_00377;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=10485882; DOI=10.1073/pnas.96.19.10661;
RA Jensen R.B., Shapiro L.;
RT "The Caulobacter crescentus smc gene is required for cell cycle progression
RT and chromosome segregation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10661-10666(1999).
RN [3]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=NA1000 / CB15N;
RX PubMed=12730166; DOI=10.1128/jb.185.10.3068-3075.2003;
RA Jensen R.B., Shapiro L.;
RT "Cell-cycle-regulated expression and subcellular localization of the
RT Caulobacter crescentus SMC chromosome structural protein.";
RL J. Bacteriol. 185:3068-3075(2003).
CC -!- FUNCTION: Required for chromosome condensation and partitioning.
CC {ECO:0000255|HAMAP-Rule:MF_01894, ECO:0000269|PubMed:10485882,
CC ECO:0000269|PubMed:12730166}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:12730166}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01894,
CC ECO:0000269|PubMed:12730166}. Note=Forms two to five small foci
CC distributed throughout the cell.
CC -!- DEVELOPMENTAL STAGE: Protein is present throughout the entire cell
CC cycle. {ECO:0000269|PubMed:12730166}.
CC -!- INDUCTION: Induced during early S phase. {ECO:0000269|PubMed:12730166}.
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:0000255|HAMAP-Rule:MF_01894}.
CC -!- DISRUPTION PHENOTYPE: Mutants show abnormal nucleoid morphology and DNA
CC segregation defects. Mutation also causes a cell cycle arrest at the
CC predivisional cell stage. {ECO:0000269|PubMed:10485882}.
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; CP001340; ACL93844.1; -; Genomic_DNA.
DR RefSeq; WP_010918261.1; NC_011916.1.
DR RefSeq; YP_002515752.1; NC_011916.1.
DR AlphaFoldDB; B8GZ28; -.
DR SMR; B8GZ28; -.
DR PRIDE; B8GZ28; -.
DR EnsemblBacteria; ACL93844; ACL93844; CCNA_00377.
DR GeneID; 7331076; -.
DR KEGG; ccs:CCNA_00377; -.
DR PATRIC; fig|565050.3.peg.376; -.
DR HOGENOM; CLU_001042_2_2_5; -.
DR OMA; HNKIAME; -.
DR OrthoDB; 1149850at2; -.
DR PhylomeDB; B8GZ28; -.
DR Proteomes; UP000001364; 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: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; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 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 ATP-binding; Coiled coil; Cytoplasm; DNA-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..1147
FT /note="Chromosome partition protein Smc"
FT /id="PRO_0000409266"
FT REGION 497..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 173..221
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 288..327
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 365..496
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 646..698
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COILED 743..880
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
FT COMPBIAS 765..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01894"
SQ SEQUENCE 1147 AA; 123273 MW; 30F881A0CA4D5779 CRC64;
MQFQRLRLSG FKSFVEPTEF RIEPGLTGIV GPNGCGKSNL LEALRWVMGA NSAKAMRAGG
MDDVIFAGSG ARPARNHADV TLTIDNADRT APAQFNDDPI LEVVRRIDRG EGSTYRINGR
EVRARDVQLL FADASTGANS PALVRQGQIS ELIGAKPQNR RRILEEAAGV SGLHTRRHEA
ELRLRAAETN LSRLEDVARE LETALNRLRR EARQAEKYKR LSSEIRAVQG AVLYARWTEA
RDHLERTTSE ATAAARLVEE TARASAAAQV AITEAEAAMP PLREEATIAQ AILGQLAIQK
DRAEREAEAA AAEFERLSND LSRIDADRAR EAQAKDDAAA ALARIAPELE EVRALVAAAP
ERGPELAAVA KAAEEARAAA EAAVEQLAAR VAAEEAQGRA AAARLSEAEA RANRTNRALE
QARAERAAVG PEVDPAAADA RQRFANAEAA LAAARAALEE AETARVKAAE QEAQARQLAR
SVEDQLGRLR TEARGLAQLT APRSKSGHAP ALDSVSPDKG YGAALAAALG DDLDAALDPK
APSYWGGAEA PAPVWPEGAE PLAPLVKAPP ALAARLSHVA VVTRANGDRL QKELKPGMRL
VSKDGDLWRW DGFVARADAP RPAAVRLEQR TRLAEVEAEI DVMAPRAEAT TIALKAAADR
LRAAEDLLRD KRRGPPDAER LLTQAREQVA KFEREQALRA ARAQSLDDTI GRFEAEKVEA
DAALGEAREA HAAAQTSGDL QPQLAEARQA AAQAREAAGA ARTALDVETR ERAGRQRRLE
SLERDRADWS KRAEAAAKRA ESLEGDRVKA AAALEAAREA PAALQEKLVA LLDEFAAAEA
RRAKASDALE TAETTRLNAD RAARAAEQAA GEAREKRAAL VAHLDGARQR FAEVASAIRE
QARMEPEELG RHVAGEAVAV PKDAAGVEAH LFALERERDA IGPVNLRAEE EAQEYAGRLE
TMRSERADLS GAVTKLRAGI EELNAEGRER LLAAFDVINA NFQTLFQALF GGGQAELKLI
ESDDPLEAGL EIFACPPGKR MASMSLMSGG EQALTASALI FGVFLANPAP ICVLDEVDAP
LDDANVDRYC NMLDEMRRRT QTRFIAITHN PVTMSRMDRL FGVTMAERGV SQLVSVDLST
AEKLVAA
