ID A0A3S0K0D0_9GAMM Unreviewed; 1164 AA.
AC A0A3S0K0D0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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:RTQ98565.1};
GN ORFNames=EKG36_18980 {ECO:0000313|EMBL:RTQ98565.1};
OS Halomonas nitroreducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=447425 {ECO:0000313|EMBL:RTQ98565.1, ECO:0000313|Proteomes:UP000267400};
RN [1] {ECO:0000313|EMBL:RTQ98565.1, ECO:0000313|Proteomes:UP000267400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11S {ECO:0000313|EMBL:RTQ98565.1,
RC ECO:0000313|Proteomes:UP000267400};
RA Yu L.;
RL Submitted (DEC-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. {ECO:0000256|HAMAP-
CC Rule:MF_01894}.
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:RTQ98565.1}.
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DR EMBL; RXNS01000024; RTQ98565.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0K0D0; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000267400; Unassembled WGS sequence.
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; 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; 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; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01894};
KW Coiled coil {ECO:0000256|HAMAP-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 3..1148
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..218
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 265..334
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 363..508
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 658..790
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 819..923
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 979..1009
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 1164 AA; 131374 MW; 3DC526010722ED72 CRC64;
MRLKSIRLVG FKSFVDPISV PFDGNMTAIV GPNGCGKSNI IDAVRWVMGE SSAKTLRGES
MTDVIFNGST GRKPVGQASI ELLFDNRDGT MGGPYAQYAE ISVKRQVTRE AQSTYFFNGQ
KCRRRDIADL FLGTGLGPRS YAIIGQGMIS RLIESRPEEL RATLEEAAGI SKYKERRRET
ENRMRRTQEN LERLEDIREE LDKQLERLKR QADAARRYQT LKQEEYRLKG ELALLRSRAL
RASQAEEEGR VRELETAVER ELLGLRQCES RLEEARADHD RLAGELEGYQ NRFHETTTAI
ARLEQDLEHT RSRDQQLARD LEAARQELAD LARLGEDDGE RLMRLDERLE TLGPEQEEVA
ERLAELEAAL EEAEPLAEEA DADWEAFGET WQADSREAER SQDRLREQEA RLERIEADAR
KRRQQREELP DIAGLSVQRD EVVERLAVLE EQLAASETRR EAWQASRDTA REAVREAEAA
REDDRQRRST LQGELASLEA LIQAALADHD ETLDDHLAAH GLAEAPRLGE CLAVTPGWED
VVSWVLAPWL RARLAPLAQA DRLLAPALAP ELGLLEAAER RTPPDTLAAK VSGAGAAAQW
LAGVRCVASR DQAWAERDAL GPGESLITAC GLWVGDGWAR HRGQDEGPDA LLVSRRREAE
VRKELAMVEA RLEAQEARLA EAAERVEQAE AGLEAVRLEE RDLEQQRQQL AVQDSGLASR
LEHLQGRAGE LAEELEGLAE SAEETRLAIE ETREHWQAAM SRLEEGAETR ERLERARQQA
RERLTQLRAQ QRPLAEQSQR LALEHQRLTT ERAGLAEQQG RAGEARERLE QRCAELEEAR
EGLHEPDEER RERLEELLHR REREERELNE ARSRAAGLVE RLREDEQARQ GHERQLEGIR
ERLQEARMQV QALTLKAETQ DEQLKELGHD SQALAEALDP NATESAWQTR LEEVGERIRR
LGAINLAAIE EYDQQAERRD YLEAQHAELS EALETLDRAI RRIDQETRSR FRDTFERVNS
GLQTLFPKVF GGGTAWLTLT GEDLLETGVA IMARPPGKKN STIHLLSGGE KALTALSMVF
AIFQLNPAPF CMLDEVDAPL DDANVGRYAK LVKEMSDSVQ FIYITHNKIA MEASERLMGV
TMQEPGVSRL VSVGVEEAAA LAEA
//
