ID   A0A0A7EIM5_9GAMM        Unreviewed;      1140 AA.
AC   A0A0A7EIM5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   11-NOV-2015, entry version 9.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   ORFNames=OM33_12335 {ECO:0000313|EMBL:AIY65827.1};
OS   Pseudoalteromonas sp. OCN003.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY65827.1, ECO:0000313|Proteomes:UP000030341};
RN   [1] {ECO:0000313|EMBL:AIY65827.1, ECO:0000313|Proteomes:UP000030341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OCN003 {ECO:0000313|EMBL:AIY65827.1,
RC   ECO:0000313|Proteomes:UP000030341};
RA   Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S.,
RA   Callahan S.M., Belcaid M.;
RT   "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003
RT   Isolated from Kaneohe Bay, Oahu, Hawaii.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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
CC       hydrolysis at each terminus and a third globular domain forming a
CC       flexible hinge near the middle of the molecule. These domains are
CC       separated by coiled-coil structures. {ECO:0000256|HAMAP-
CC       Rule:MF_01894}.
CC   -!- SIMILARITY: Belongs to the SMC family. {ECO:0000256|HAMAP-
CC       Rule:MF_01894}.
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DR   EMBL; CP009888; AIY65827.1; -; Genomic_DNA.
DR   RefSeq; WP_038642101.1; NZ_CP009888.1.
DR   EnsemblBacteria; AIY65827; AIY65827; OM33_12335.
DR   KEGG; pseo:OM33_12335; -.
DR   KO; K03529; -.
DR   Proteomes; UP000030341; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030261; P:chromosome condensation; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP.
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; IPR011890; SMC_prok.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_01894, ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000030341};
KW   Cytoplasm {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:UP000030341}.
FT   NP_BIND      32     39       ATP. {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   COILED      170    380       {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   COILED      170    218       {ECO:0000256|SAM:Coils}.
FT   COILED      272    299       {ECO:0000256|SAM:Coils}.
FT   COILED      314    334       {ECO:0000256|SAM:Coils}.
FT   COILED      342    376       {ECO:0000256|SAM:Coils}.
FT   COILED      411    503       {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   COILED      426    493       {ECO:0000256|SAM:Coils}.
FT   COILED      642    724       {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   COILED      647    667       {ECO:0000256|SAM:Coils}.
FT   COILED      696    723       {ECO:0000256|SAM:Coils}.
FT   COILED      784    879       {ECO:0000256|HAMAP-Rule:MF_01894}.
FT   COILED      787    814       {ECO:0000256|SAM:Coils}.
FT   COILED      836    877       {ECO:0000256|SAM:Coils}.
FT   COILED      916    977       {ECO:0000256|HAMAP-Rule:MF_01894}.
SQ   SEQUENCE   1140 AA;  128606 MW;  F74FE41ECE99889F CRC64;
     MRLASIKLAG FKSFVEPSKI PFPDQMTCVV GPNGCGKSNV IDAVRWVLGE SSAKNLRGDA
     MTDVIFNGST ERKPVSQASV ELLFDNTEGR LPGTLASRNQ IAIKRLVTRE GVSQYYLNGE
     KCRKRDITDI FLGTGLGPRS YAIIEQGMIS RLIESKPQDL RIFLEEAAGV SKYKERRRET
     QTRLNSTRDN LERLLDLRNE LENQLNVLTE QADKARIYTT AKSKERTLKA QICVLKWQSL
     QQKLLESEAK LSDIDEQIGF LTEAHTGHDD VISALKLAIE QANDLLNDAQ HQEFQLRNKL
     ARDEQDKIHK QAQKVQLSQR IGQLQKQFKQ LDQDQLETKD NYQDQQEQLA LCQAELEQYE
     ELVELSLAKY EEQKAQQDEL YSAYQVSLGD NNGLVQEQQS LQSSLSSLEV QEARFTQQKL
     AQCEQKAALQ EQYVTLETKL ATFKLDQIQA RHEQVSNNLS ELNGEVATAQ KALAEKHTQM
     TEAEHQLQSL LTKRDALALV LNEHNDNSSS VANLLPSLKV GQDWHLAVEA SLFNLRFAHR
     VEQLDQDLIQ PQIWQQAMQV TIGSLAEKVM EGAYPSYFNL IAVVDDVNAL NDDFWQGEFH
     FAVDSKGNLR GDNWFLPCQF DHDNSLLVKH QLLKEIELSI PESELQLQSA QKTLTAQQSL
     VESLQSQQKE LNSAFALIDR ELTQSRAEYS FSEKRFDEIN LQLNTVSNKQ AELEAQLQLL
     SDNKTPLVTE LEDIIKKQAE SKERQTHFEA AYHNAKLVTR QLQTAFEGEK SQCHKVQLHL
     QTMQNQIVLS ESKLNQFSTR YDELNEQLEE AKLTLEDVQM PLVELDETIA EQHLLLEQQI
     EQKQQKQLAL EDAKEKLKQA ESGIGSEQEK LESLKQTKQS IVLEQQSFQL KSEAALAPLA
     ELNTQLKDVI ADLPEDTKLT TLQGQLSKVS NEISQLGAIN LAAIEEFDKA SARKNYLDQQ
     YDDLVSALET LESAIIKIDR ETKQRFKATF DQVNSGLQDL FPKVFGGGSA YLELTSDDLL
     ETGVAIMARP PGKKNATIHL LSGGEKALTA LSLVFSIFQL NPAPFCMLDE VDAPLDDANV
     GRFCRLVEEM SQDVQFVYIS HNKIAMEMAA RLTGVTMAEP GVSRVVAVDI EKALEMSESA
//