ID A0A074L0W6_9BACT Unreviewed; 1179 AA.
AC A0A074L0W6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=EL17_22980 {ECO:0000313|EMBL:KEO75886.1};
OS Anditalea andensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO75886.1, ECO:0000313|Proteomes:UP000027821};
RN [1] {ECO:0000313|EMBL:KEO75886.1, ECO:0000313|Proteomes:UP000027821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY1 {ECO:0000313|EMBL:KEO75886.1,
RC ECO:0000313|Proteomes:UP000027821};
RA Yang L., Wei S., Tay Q.X.M.;
RT "Characterization and application of a salt tolerant electro-active
RT bacterium.";
RL Submitted (APR-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. 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:KEO75886.1}.
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DR EMBL; JMIH01000004; KEO75886.1; -; Genomic_DNA.
DR RefSeq; WP_035068917.1; NZ_JMIH01000004.1.
DR AlphaFoldDB; A0A074L0W6; -.
DR STRING; 1048983.EL17_22980; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000027821; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027821}.
FT DOMAIN 520..628
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 188..215
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 255..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 664..731
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 774..864
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 893..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 1179 AA; 136099 MW; B7E753E415779408 CRC64;
MQLSKLEIKG FKSFGDRVVI HFDKGITGIV GPNGCGKSNV VDAIRWVLGE QKTRMLRSDK
MENVIFNGTK NRKPTNLAEV SLTFENNKNL LPTEYTQVTI TRRYYRSGES EYLLNGITCR
LKDITNLFMD TGINSNSYAI IELKMIDELL NDKNNSRRDL FEEAAGISKF KTRKKETLRK
LEDTDGDLSR VEDVLFEIEK NLKQLEKQAK QTEKYFTVKK EYKAASIALA KKSVNKHTTA
LVQMSASITQ EQDRKLSLNA KVAEQEALLE KNKNELLLKE KLLSARQRSL NEQVNKIRQF
ESDKKIKNER LRFLEDRGQK LREQIDLDRK SNDRAGFSIR SLQQEKESAE KLLREKEFVV
DNLKTELQEQ KDTYALSQER QKVLNKEFTS RKETIYQLSK DLEIKQIQLS TLKQELEKTA
TDDDNQEANL AEFEEKVVLL KEELDLRTDA LHELKKKEED QLARIEEAVH TIDLIKDEVT
QSSRKLDAKQ NEYNLTKSLV ENLEGFPEAI KFLKKNSSWG KDTPLLSDIL TTEEKYRVAI
ENFLEGYMNY YVVETEAQAI AAVNLLSDAA RGKANFFILE HFERFQPSVT KLFPNVIAAT
EIIEYDLKYS KLISFILDDV YIIKGEYRDI PLDHTSVFIT ESGKLTKRKF SISGGSVGLF
EGKRIGRAKN LEKLEKDIKE LNKKVSQTRS DLDRKMGDLM KLKEVSHKSQ IEVLQNEINE
YNQQYISVRT KKEQLFELLS TNANKREDIL IRIDSLSEEV AELLPSLDAS KSGFSELEYE
LEEINENLQV ESESVSLKSN LFNQENILYH QHINKVNSLE QEIDFKQNAF ETSKERIEKS
QHELSGIEQE VKNLLDNNEI KDDELIELYT EKEQIEIGVN EAEKAYYAYR GNIDEIEKAL
REIQKQKEHI DTIIMELQQS LNEVKLKLSG MKERLSVEFE IDLDTLMEED PEISPEYADW
DDHQLRTEVA KAKEKLDKIG PINPMAMEAY NEIKERHTFI TEQKEDLIKA KNSLLETIKE
IDQVAKTTFM DAFDKIKENF IKVFRSLFTA EDDCDLKLTD PTNPLESTIE IMAKPKGKRP
LTINQLSGGE KTLTATSLLF AIYLLKPAPF CIFDEVDAPL DDANIDKFNN IIQTFSSESQ
FIIVTHNKRT MASTDIIYGI TMIEAGVSRV VPVDLRELV
//
