ID A0A101D1V2_9GAMM Unreviewed; 1164 AA.
AC A0A101D1V2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=XD36_2148 {ECO:0000313|EMBL:KUJ87440.1};
OS Halomonas sp. 54_146.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1635257 {ECO:0000313|EMBL:KUJ87440.1, ECO:0000313|Proteomes:UP000053192};
RN [1] {ECO:0000313|Proteomes:UP000053192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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:KUJ87440.1}.
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DR EMBL; LGEN01000023; KUJ87440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101D1V2; -.
DR STRING; 1635257.XD36_2148; -.
DR PATRIC; fig|1635257.4.peg.1870; -.
DR Proteomes; UP000053192; 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; 1.10.287.1490; -; 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; 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; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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..1149
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 765..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 265..306
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 349..466
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 855..914
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 980..1010
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 769..789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 131743 MW; C0F87EC344D9DCF7 CRC64;
MRLTSIRLVG FKSFVDPVTV PFDGNMTAIV GPNGCGKSNI IDAVRWVMGE SSAKTLRGES
MADVIFNGST GRKPIGQASI ELKFDNRDGS MGGVYAQYAD IVVKRLVTRD GQSNYFFNGQ
KCRRRDIADL FMGTGLGPRS YAIIGQGMIS RLIEARPDDL RATLEEAAGI SKYKERRRET
ENRMRRTQEN LERLDDIREE LDKQLERLKR QAEAAKRYQE LKQLEYRLKG ELALLRGRTL
RSEQSHQESR VRELEIAVEK EVFGVRQCET RLEQAREQHD ELAEVLDRHQ QQFFETTTRI
ARLEQDQAHR RSREAQLASD IATARRELDE QRQISAGDQQ RLIAIDERFD DLHPEHEALE
EQLESLEQAL ADASPALEAA EQQWADAETR WRDASRDAER SQDQLRDLEQ RIARLQTENQ
RRRQQHNEVA DLTVLREEHA VCEAQLTDAQ QQAEGFQTQR DQWQQRYGDA KAAYQQAVQA
RDQQRAELSQ RQGELASLQA LIDAALVDHD PAIGTTLAAH GLADAPQLGE VLQVEPGWEA
LVSWLLAPWL NARLVASHQL AALPEALAAD WRLIDHTPLT ANPSGQRLDS LVKGAGALGE
WLASIHYTQT AEQAEQQVAN LAPGESVVSR DGVWRGRGWL HQQANGEGID GLLLTRRRYA
ELNAQREQQE QALALAEEQC EAASETIEAL EQTREQQAEQ ERTHAATLQQ LAVKERSLAQ
RLEHLESRAT ELDEELAQLQ EDEAELALTI DEQRARWHVA MEQLESSAEA RETSAEQRNR
QREARDQLNQ QHAPLKAQQQ ALALERERLS AERDSLRAQQ SRSSDSEERL SLRIAELEET
REMLIEPDEL AGEELEELLH QREQQEGRLN ATRQQAQALA EQLRTDELAR QQHERNLEQT
REQLQQRRMD VQALALKAAT QDEHLAELGH NAETLAEQIP PEASEAGWQE RLEATTDKIR
RLGAINLAAI EEYDQQAERR NYLEAQHAEL TEALETLERA IKRIDQETRV RFRETFDQVN
AGLQALFPRV FGGGAAWLTL TGDDLLETGV AIMARPPGKK NSTIHLLSGG EKALTALSLV
FAIFQLNPAP FCMLDEVDAP LDDANVGRYA RLVKEMSENV QFIYITHNKI AMEAAERLMG
VTMQEPGVSR LVSVGIEEAA ALVD
//
