ID Q1GQU3_SPHAL Unreviewed; 1147 AA.
AC Q1GQU3;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Sala_2270 {ECO:0000313|EMBL:ABF53979.1};
OS Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS (Sphingomonas alaskensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF53979.1, ECO:0000313|Proteomes:UP000006578};
RN [1] {ECO:0000313|EMBL:ABF53979.1, ECO:0000313|Proteomes:UP000006578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13593 / LMG 18877 / RB2256
RC {ECO:0000313|Proteomes:UP000006578};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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; CP000356; ABF53979.1; -; Genomic_DNA.
DR RefSeq; WP_011542555.1; NC_008048.1.
DR AlphaFoldDB; Q1GQU3; -.
DR STRING; 317655.Sala_2270; -.
DR KEGG; sal:Sala_2270; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_3_5; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006578; 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 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; 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:UP000006578}.
FT DOMAIN 3..1130
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 172..276
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 372..510
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 647..730
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 828..876
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 951..985
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 1147 AA; 121135 MW; 529DDF3C2E74AA48 CRC64;
MQIKRLRLTG FKSFVEPTEL RIEPGLTGVV GPNGCGKSNL LEAIRWVMGE SSPKSMRGGG
MEDVIFAGTS SRPARDFAEV ALHCDTEGAL VAGLSDGGDG DDLEIIRRIE RGAGSAYRAN
GRDVRAKDVA LIFADAATGA HSPALVSQGK IANVIAAKPT DRRAMLEEAA GIAGLHVRRK
DAEQKLRATE TNLTRLSEIV ADMEVRAATL RRQARAAEKY KKLSDDIRIA EARLIYARWR
DAAAAADQAR RDADAAEAAV KAAQDELETI AKAQAEVAAR VAAARSDAQA RRDALAEATA
TQLRLQSEER AALQRLDDLA AQQRRIEADR AHEGELAREA HAALTALDAE TKSLAQDIAG
HDASKAALAD ANFAAQARLR DAEVALAQAR AKAASEAADR RIAASARDSA EAAVRRIAAD
KARIEAEIAA LGDSAALAAT HAESLAAAEA AEAAIATAEQ ALYDAEAERE ATATELARVE
AALAEARAAL AALDGEATTL ERALAAAQSD DDRILDRLRA QPGYEAALAA ALGDDLDAGT
DPAAARSWTG AAAARDDPAL PAGTTPLAAH VQAPAALARR LAQVAVAETD GGQPLAVGQR
LVTLSGVMRR WDGFVTRGDG ATATERLQRR NRLDELAAQR PAVELGVQEL RDRREAAATK
AAALTEAAAA ARKALADADA ARRTALRAAD QAQAALDRHR DAAALLARRL AEVAETAKDA
DAQLAAQEAA LAALPDEAIG RAALAAGEQA ADRARANANS ARDALAAHDR TLAALSERQA
VVSAEIKSWK ARAGEAARRV TEMDKRADAL AAEAAKLADA PARLAEQRAA AEAEQASLRE
KVAAAEAQER AAEAALREAE TALNAIRERV AAARETRAGA AARSENAELR RVEMGRLSGE
RFECPPPLLP QKAGFESESI GDPQAESAAH DRLVADRERL GPVNLVAADE LAELDAEREK
NAAEIEELTQ AVHRLRGSIG NLNREGRVRL LAAFETVNTH FQRLFSTLFN GGQAHLELVD
SDDPLEAGLE IMAQPPGKRL GTLTLLSGGE QALTAIALIF GLFLTNPAPI CVLDEVDAPL
DDANIERFCD LLDRMARETN TRYLIVTHNA VTMARMHRLF GVTMIERGVS RLVSVDLGGA
EELLAAE
//
