ID   A0A0A7EIM5_9GAMM        Unreviewed;      1140 AA.
AC   A0A0A7EIM5;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   03-AUG-2022, entry version 28.
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 piratica.
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., Callahan S.M.,
RA   Belcaid M.;
RT   "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT   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 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; CP009888; AIY65827.1; -; Genomic_DNA.
DR   RefSeq; WP_038642101.1; NZ_CP009888.1.
DR   STRING; 1348114.OM33_12335; -.
DR   EnsemblBacteria; AIY65827; AIY65827; OM33_12335.
DR   KEGG; pseo:OM33_12335; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_6; -.
DR   OrthoDB; 1149850at2; -.
DR   Proteomes; UP000030341; Chromosome 1.
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; IPR011890; SMC_prok.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   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:UP000030341}.
FT   DOMAIN          3..1123
FT                   /note="SMC_N"
FT                   /evidence="ECO:0000259|Pfam:PF02463"
FT   COILED          170..218
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          272..376
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          426..493
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          696..723
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          787..877
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   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
//