ID I8RF27_9FIRM Unreviewed; 1185 AA.
AC I8RF27;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=FB4_3527 {ECO:0000313|EMBL:EIW18053.1};
OS Pelosinus fermentans B4.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW18053.1, ECO:0000313|Proteomes:UP000004324};
RN [1] {ECO:0000313|EMBL:EIW18053.1, ECO:0000313|Proteomes:UP000004324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:EIW18053.1,
RC ECO:0000313|Proteomes:UP000004324};
RX PubMed=22933770; DOI=10.1128/JB.01174-12;
RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL J. Bacteriol. 194:5147-5148(2012).
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:EIW18053.1}.
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DR EMBL; AKVJ01000028; EIW18053.1; -; Genomic_DNA.
DR RefSeq; WP_007934569.1; NZ_AKVJ01000028.1.
DR AlphaFoldDB; I8RF27; -.
DR PATRIC; fig|1149862.3.peg.2487; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000004324; 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 Gene3D; 1.20.1060.20; -; 1.
DR Gene3D; 3.30.70.1620; -; 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}.
FT DOMAIN 522..640
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 234..387
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 416..499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 766..863
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 899..933
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 1185 AA; 134909 MW; 37958EC8E39538A0 CRC64;
MLLRRLEAYG FKSFADKTEI EFGNGITAIV GPNGSGKSNI SDAIRWVLGE QSVRNLRSTK
MEDVIFSGSL GRRPLGAAEV SVIFDNSDGT LPLDFSEVII TRRVFRSGDS EYFINKAACR
LKDIYELLAD TGLGRDAMTV IGQNKVDEVL NSKPEERRLL FEESAGISKY KQRKKDAMRK
LEDTTQNLIR VSDITNEIED QLVPLRESAE KTKQYNTLKT ELTSCQVTLL LSTLDKSEKI
IESANLQKEH LTENELTVST NLNLKETDKE KLATELIQVE EKLISYTTFI NEAETELERI
RGKVAVLEER ISQGKRNQER IRDEEIRVGK QKDELEKKNS EVNEILIEKK KFTENLQQIL
IDKNVLYQNV VTNLEQAEKQ LESSKDKTLT FLQEIVEERN RLVTIKNDIV RSETRERSFD
QEYQDYQTQL QQAESAYTSL LAEQEAIQVK ITQLNQENNA LHIKKKSTED TLQQFLHQEQ
QLTRQVNELQ SRFKILSNMQ NDYEGFARGI KSILKSNAPW QKGIWGAVAQ TITVPDEYVM
AIEIALGGAL QYIITEDSDI AKEAMHFLKT ERLGRATFLP LNTIKPFKPR DTEITAAKMK
GSLGFAADLV TCDSRYRKVI EFLLGRTIIA KDVDIALTIA NQSGFSVKIV TLDGEVLNPG
GSMTGGSTGK RETSFLGRNN EIAAIKLKLD EGRKSFEAIQ EKVINVRAEV QNINYELAAI
QEQRQQMDVR QAEITVHTDK MQFDIKRVTL AITTINTDRA ACSREKEQLE VTLSQCKARI
VSLENRDGQH KQTIALEQQK CKELQASKDI LQESLTDLKI NITTVQQEIA GFVANCEQAE
QAKQLLQEQL QQLFAERTDI AAQILQSSQE LSDTSSKFKT LTEEKINYEQ HNKNHYGIKL
NLLVEMQQLE KELKDLRRNH HEVQTRLHES ELLATKYSFE VTRCLEQLEQ KFCLTIDQAK
ELCRTESLDS INKLIKNLEK ELMILGPVNH GAVEDYIRLQ ERCDFLKNQF QDLTSAKEYL
ASIIADIDKT MSTKFLIAFT KINEHFCDIF SRLFGGGQAQ LKLVDPDNIL HTGIEISVQP
PGKKMQNLIL LSGGERALTV IALLFSFLAY RPAPFIVVDE IDAPLDEANI DRLREFLRDY
ARHTQFIVVT HRKGTMEAAD IIHGITMEQS GISRLVSVKL TDEIK
//
