ID A0A0A7EIM5_9GAMM Unreviewed; 1140 AA. AC A0A0A7EIM5; DT 04-MAR-2015, integrated into UniProtKB/TrEMBL. DT 04-MAR-2015, sequence version 1. DT 29-SEP-2021, entry version 26. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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: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 NP_BIND 32..39 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894" FT COILED 170..218 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894" FT COILED 272..299 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894" FT COILED 342..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..814 FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894" FT COILED 836..877 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 //