ID A0A386HQN9_9BACT Unreviewed; 1174 AA.
AC A0A386HQN9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:AYD47574.1};
GN ORFNames=D6B99_08130 {ECO:0000313|EMBL:AYD47574.1};
OS Arachidicoccus soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=2341117 {ECO:0000313|EMBL:AYD47574.1, ECO:0000313|Proteomes:UP000266118};
RN [1] {ECO:0000313|EMBL:AYD47574.1, ECO:0000313|Proteomes:UP000266118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIS59-12 {ECO:0000313|EMBL:AYD47574.1,
RC ECO:0000313|Proteomes:UP000266118};
RA Weon H.-Y., Kwon S.-W., Lee S.A.;
RT "Arachidicoccus sp. nov., a bacterium isolated from soil.";
RL Submitted (SEP-2018) 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}.
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DR EMBL; CP032489; AYD47574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A386HQN9; -.
DR KEGG; ark:D6B99_08130; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000266118; Chromosome.
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; 1.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000266118}.
FT DOMAIN 520..631
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 167..380
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 420..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 732..850
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 889..934
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 1174 AA; 134253 MW; F9F566E213FB18A1 CRC64;
MRLKQLEVKG FKSFADKTIV NFDEGITGII GPNGCGKSNI IDSIRWVIGE QKISALRSEN
LEALVFNGSK SRSASGLAEV SLTFENTRNL LPVEFSTVTI TRRFYKNGDS EYRLNDISCR
LKDIQNLFMD TGISTDSYAI IELGMVDDII KDKENSRRRM LEQAAGVTVY KTRKKEAKQK
LDATEQDLNR IEDLLFEINN QLKTLENQAK KAEKYFEIKK DYKEISIELA KAALEGFNLS
YRELQEKTSL EADKKNQLEQ EIEAEEEALQ NEKAKYIDQE EALSEMKSSF NELQQNLRSK
ENEKNLAAQK LQYLREKETG LHSFLQKAEG QLGNLKESIE FTQEQIGDEE VLQAELIEKL
EIAKEQIEEK RIVFEEKRTN AESLRSGHLA AQRNQFDAEK KVAVADTSIQ NLTRSQAQLM
SETEHRKSEL QSLQTQLEEK EALLENGRAE LLNLREQHET AKASIFSAQE ELEAMRSELA
EESRTLDSKR NEQALLKSLI DSMEGYPESI KFLHKNKDWH HEAPILSDII YVEEDYRAAL
ENVLEPYLNY YVVKNLEQGL QAIHLLDNNK KGKANFFLLD KIENFVTETR HIPNATCAMD
VIEVDEPYHK LAQYLLGNVF IAENEQSIDN ANVASVILLE KSGKFVKGNY TLSGGSVGLF
EGKKIGRAKN LEKLNDEIVL QDAVVNALKT QIQKKQSDVL HFNEQLKDKE IRERENDTNQ
LTNQVFATKN KIENLQLSQQ NAIQKLDEIE EKIAEEKEAI AATREDLTAF DEQLKQLSEE
IQIIQRDYYQ AEQEFNFATA AFNDFNLQST RQQSKMAALK QELVFKENQL KDLQQQIENN
ANQLKNSSVE ITEAEQFLVE STQLFEALSQ QKIKDEEALR IADSSYYGIR KLLSEKEEAL
KLKSKQRENI DHILNEMKDK LNELKLQLAG MKERLSVEFK VDLDQILDEA RKTNTPLEDL
QISTERMKKR LENMGEVNPT AIEAFTEMKK RYEFILEQKN DLVTAKESLL QTIQEVEATA
NQQFLTTFNQ VRENFQKVFK ALFSEEDTAD MVLANPENLA ETGIDIMAKP KGKRPSSISQ
LSGGEKTLTA TALLFAIYLI KPAPFCILDE VDAPLDDANV GKFTQMIQKF SQNSQFIIVT
HNKQTMSAVD VIYGVTMQEA GVSKLVPVDF RSLN
//
