ID D4ZIY3_SHEVD Unreviewed; 1136 AA.
AC D4ZIY3;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=SVI_1661 {ECO:0000313|EMBL:BAJ01632.1};
OS Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ01632.1, ECO:0000313|Proteomes:UP000002350};
RN [1] {ECO:0000313|Proteomes:UP000002350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC {ECO:0000313|Proteomes:UP000002350};
RX PubMed=20458400; DOI=10.1039/c000396d;
RA Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA Nakasone K., Mori H.;
RT "Complete genome sequence and comparative analysis of Shewanella violacea,
RT a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL Mol. Biosyst. 6:1216-1226(2010).
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; AP011177; BAJ01632.1; -; Genomic_DNA.
DR RefSeq; WP_013050939.1; NC_014012.1.
DR AlphaFoldDB; D4ZIY3; -.
DR STRING; 637905.SVI_1661; -.
DR KEGG; svo:SVI_1661; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000002350; 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 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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002350}.
FT DOMAIN 3..1119
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 666..714
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 1136 AA; 127532 MW; E98B32E9EF7C1D99 CRC64;
MRLKQIKLAG FKSFVDSTKI PFLNPLSAII GPNGCGKSNI IDAVRWVLGE SSAKHLRGDS
MADVIFNGST ARRPVSVASV ELSFENLDGR LMGEYSSYQE IAIKRQVSRD GDSSYFLNGQ
KCRRKDITDL FMGTGLGPRS YAIIEQGTIS RLIESKPQEL RVFIEEAAGI SRYKERRRET
ENRIRHTREN LDRLGDIRNE LGRQLEKLAE QASEAKQYRE LKQSERQLDS ELFVSRYLEL
IHQTERLTLD VNRLELAKAE VEAEKERTEL ELTRLNVQLV ELDGEEQKRV ESFYLSGTQI
AKLEQELKHR QQQDSHVEQR ITGIVHKLNQ HKDKLSSDET SQQALSEELV LKRPQIEQTH
LSLTQVTADL SAHELKAAES RTLLSEHKEK VSSYRLAYEV SRGKLSHQGI MLEQTRAQLS
SIEQDAAGLL KQEDVKIGQD NLGRLTQWQI DAMEQGEIND ELDQKLTDLL QSQVNLKAKQ
EALSQSLAEE RGRLALITKL LLDDENQSGA KALWQLINVQ PGWEKAVELI FDGLLKMPAG
VEKGEFGFEG LISQEWHGMS SNANLSPWLS LIRWAETLEQ ARELVSGISE HERIVTADGY
LLGKGFVIKK GTDSGSLVQL KREQEALDVS IDDSEALLSE LNNQGHGLDA NITPLKIELA
SGIDTLQKLN VSIARLTVQI EADKQRNKDL SQRREHLVSE LARLKVLLNK QQEDEVSVLA
NLDNAQSSLK QGEQAQTSLV KGLDEQVDSV GVFKDKYQQV QQADRDLSQV CQTLTTKLAL
NEQSINQQRV RIEELTLAKS ALEHQLVEQN VASEDGQLSS LKEQLGQALA QQQTKQVELA
RLRQQQTKLQ ESCDSSGIKK KQQLGKTEDL TQSISTLKLR REGLKGQADS QLMQLKEQDI
ELEQVKSSLD LKKSSQVRQR ELERIRAQII HLGAINLAAI EEYEQQGERK NYLDSQDEDL
TSALTSLEEA IRKIDKETKS RFKDTFDKVN KDLGILFPKV FGGGSATLAL THDDLLEAGV
TIMARPPGKK NSTIHLLSGG EKALTALSLV FAIFRLNPAP FCMLDEVDAP LDDANVDRFC
RLVKEMSQTV QFIFISHNKL TMEMADQLIG VTMHEPGVSR IVAVDIDEAV ALADAG
//
