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Database: UniProt
Entry: C4IJE9_CLOBU
LinkDB: C4IJE9_CLOBU
Original site: C4IJE9_CLOBU 
ID   C4IJE9_CLOBU            Unreviewed;      1187 AA.
AC   C4IJE9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN   Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN   ECO:0000313|EMBL:EEP54856.1};
GN   ORFNames=CLP_2538 {ECO:0000313|EMBL:EEP54856.1};
OS   Clostridium butyricum E4 str. BoNT E BL5262.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP54856.1, ECO:0000313|Proteomes:UP000003081};
RN   [1] {ECO:0000313|EMBL:EEP54856.1, ECO:0000313|Proteomes:UP000003081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA   Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA   Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.;
RL   Submitted (AUG-2009) 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. SMC3 subfamily.
CC       {ECO:0000256|ARBA:ARBA00005917}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEP54856.1}.
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DR   EMBL; ACOM01000005; EEP54856.1; -; Genomic_DNA.
DR   RefSeq; WP_003415523.1; NZ_ACOM01000005.1.
DR   AlphaFoldDB; C4IJE9; -.
DR   STRING; 1492.ATN24_07495; -.
DR   eggNOG; COG1196; Bacteria.
DR   HOGENOM; CLU_001042_2_2_9; -.
DR   Proteomes; UP000003081; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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; 2.
DR   Gene3D; 1.20.1060.20; -; 1.
DR   Gene3D; 3.30.70.1620; -; 1.
DR   Gene3D; 6.10.140.1720; -; 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; IPR010935; SMC_hinge.
DR   InterPro; IPR036277; SMC_hinge_sf.
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; PF06470; SMC_hinge; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   PIRSF; PIRSF005719; SMC; 1.
DR   SMART; SM00968; SMC_hinge; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF75553; Smc hinge domain; 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:UP000003081}.
FT   DOMAIN          525..642
FT                   /note="SMC hinge"
FT                   /evidence="ECO:0000259|SMART:SM00968"
FT   COILED          167..194
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          245..289
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          318..516
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          733..802
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          873..944
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT   COILED          992..1033
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   1187 AA;  136469 MW;  82C279EB8FCCF7B4 CRC64;
     MFLKSLEIRG FKSFADKTEL KFKKGVTAVV GPNGSGKSNI SDAVRWVLGE QSIKVLRGGK
     MEDVIFAGTQ FRKPVGLAQV SLTLDNSDEQ LATEYNEVTV SRRIFRSGES EYLINNNKCR
     LKDVTNLFMD TGIGKEGYSL IGQGKIEAIL SGKPEERRAL LEEAAGIVKF KNRKEEAEKK
     LSNTDDNLVR INDILSTYEE RIEPLRIERE KAIEFKELSD NLKRKEVSLI VHTIQIMDQE
     LRVFKEELNK RIEGINKKRE SIAKDKEILS NLEERIENIE KKTLGEKEQY YTLKDIINDD
     GKAIELYHER IKNCEEKIKR NSYEVEDISK RMEDIENNKL LLEQELAKRF EEQADKKEII
     EKLEQTNKIK QLELEKMKAE LKVLQKSELD FLRSNSDVKN EINILKRELE LREEKRQSLD
     SSISYLENNI VINMATYKVL SRDIDNKKKE IEDVRNSTAE LKKRIATLKG NITKKENDVK
     ELNRVLTKLD ANKTMLENLE KHYEGYNRSV KSLMESIKDE NIEGAEETKV LGEVFSVDKQ
     YETALEIALG AAISNVITST EQVAKKLIIY LKKNNLGRAT FLPINIIKGK KLNLDDSITK
     SEGYIGIGSD IISYDSIYEN IMNYTLGRTI ICRDMDCALK ISKISQYRYK IVTLEGEVVN
     PGGALTGGSI KGRNTNLLGR KREIEEIAHK IDEKKKVYAD IMKEGQKLSL ELKEIDEEIL
     NNTDLIHSKN IDLTRKQSEI EGLQNDTNKL KKTLENTRID LERIKEDKQE ISEKLNIKEN
     EIRILEDENV TKKNQSVELE ELIGVKTLEV SKDESKLTEM KIAKAALDEG IEGKKNDFSR
     IEKESYDLSG KRDNLVRESK ENEKSIIELN FSIKERQKNI EENNTKINIL ELNFKDDEIE
     KEKLKEEFKQ KDNLISAVMD EISREEMEVN KREVIKAKKE SEEEHIYKKL NEELELTYAE
     ALDICEPVEN EEDLKSNISS IKSKITKLGI VNLAAIEEYE ELKEKFEFMS NQAEDLEKAK
     EELIRVIDEM TGEMRILFKE NFKILNHNFN ETFKDLFQGG SAELILGEGD ELSANIDINV
     EPPGKKLQNI NLMSGGEKVL SAIALLFAIL KMKPTPFCIL DEIEAALDDA NVYRYAEFLL
     RFSNRTQFIV ITHRKGTMEA SDIIYGVTME EKGISKVVSV DLSKDDE
//
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