ID B8CN89_SHEPW Unreviewed; 1141 AA.
AC B8CN89;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=swp_1966 {ECO:0000313|EMBL:ACJ28723.1};
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ28723.1, ECO:0000313|Proteomes:UP000000753};
RN [1] {ECO:0000313|EMBL:ACJ28723.1, ECO:0000313|Proteomes:UP000000753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753};
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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DR EMBL; CP000472; ACJ28723.1; -; Genomic_DNA.
DR RefSeq; WP_020912098.1; NC_011566.1.
DR AlphaFoldDB; B8CN89; -.
DR STRING; 225849.swp_1966; -.
DR KEGG; swp:swp_1966; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000000753; Chromosome.
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; 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; 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; PF02463; SMC_N; 2.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|HAMAP-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 3..355
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 667..1124
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 265..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 685..719
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 783..817
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 865..892
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 1141 AA; 127848 MW; FD6F23398549C5A9 CRC64;
MRLKQIKLAG FKSFVDPTKI PLPNPLSAII GPNGCGKSNV IDAVRWVLGE SSAKHLRGDS
MADVIFNGST ARRPVSVAGV ELLFDNQDNR LAGQYASYQE IAVKRQVSRD GDSSYFLNNQ
KCRRKDITDL FMGTGLGPRS YAIIEQGTIS RLIESKPQEL RVFIEEAAGI SRYKERRRET
ENRIRHTREN LSRLGDIRSE LHKQLERLAE QAQTAKQYRE LKQSERQCES ELVVSRYHEL
NQQTDTLTVQ IGKLEVQQAS LLAEKQTLEL SLTELNLKLS ELDSQEHQQV EAFYLTKTHI
AKLEQSLKHR EQQDDSLNQR LAEISAQIAL QQASLKTANA NQEKLLKQQQ ELAPEINAWQ
QKTSSQSAEL ALVSQRHIAS TEQFQLHSGD EAKAHLAVEM NRTQLTHCSK ELTHKQQSVA
RLTQRALEHR EQLAELKGSS LANQCETLSI ETEQAQEVYD ELSFNIETRQ QSCDELKTEL
ESVKVKLADE TGRLSVVTQL LPDEGDEGDT RLWQVIEVSP GWESVVDLLL ANVLNSPVLA
ELSTEASIGF SANTLASGVV NDVIQSPVNL NPWLSQVKWL ETKDEAIQRR KELGAEQMFA
TADGFLVGAD FIIEKSADSG SLVQLKNEHV ALTEVVCDTE ERLSFLTQTL SVHIEELKPQ
LILQQQQYQQ IQAQKVALAG MASQVKAMQT TINDTDARYK QLQQELAETE TELQQLITQQ
AQFLHSEANL QQAFELVSKS RQAAESDKLS AFKSLSELKD LLNGSELRLK ASLKSEQAIQ
TQVALIEQTV SHQKQRLEEL ELNKEQVRLQ LDNKEDVDTA QNSQSLKTQL AQALEAQQVK
QQALNLLRQE QAGLQELCDS AGTNKKQQLA KIEDLTQTMS ALKLRREGLK GQIDSQFSLI
TEQGIDVEQV LSKLDASRNT LWRQKELERL RARIAHLGAI NLAAIEEFEQ QNQRKSYLDS
QDEDLNSALG SLEEAIRKID TETKSRFKDT FDKVNKDLGI LFPKVFGGGS AYLALTDDDL
LETGVTIMAR PPGKKNSTIQ LLSGGEKALT ALSLVFAIFR LNPAPFCMLD EVDAPLDDAN
VERFCRLVKE MSQSVQFIYI SHNKITMELA DQLIGVTMHE PGVSRIVAVD IDEAVALADA
G
//
