ID K0CC23_ALCDB Unreviewed; 1169 AA.
AC K0CC23;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:AFT70050.1};
GN OrderedLocusNames=B5T_01773 {ECO:0000313|EMBL:AFT70050.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT70050.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT70050.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(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}.
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DR EMBL; CP003466; AFT70050.1; -; Genomic_DNA.
DR RefSeq; WP_014994122.1; NC_018691.1.
DR AlphaFoldDB; K0CC23; -.
DR STRING; 930169.B5T_01773; -.
DR KEGG; adi:B5T_01773; -.
DR PATRIC; fig|930169.3.peg.1750; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000006286; 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; 2.
DR Gene3D; 1.10.287.1490; -; 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; 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:UP000006286}.
FT DOMAIN 520..621
FT /note="SMC hinge"
FT /evidence="ECO:0000259|SMART:SM00968"
FT COILED 170..225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 300..500
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 655..907
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 977..1014
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 1169 AA; 133321 MW; F692DE05E4CF6EB3 CRC64;
MRLKSIKLAG FKSFVDPTTA LFPDNLTAVV GPNGCGKSNI IDAVRWVMGE SSAKHLRGES
MADVIFNGSN SRKPVAQASI ELVFDNAEGK IQGEYGKFSE ISVRRLVTRD GQSNYFLNGA
KCRRKDISDI FMGTGLGPRS YAIIEQGMIS RLIEAKPEEL RVYIEEAAGI SKYKARRRET
ENRMRRTREN LERLTDIREE LERQLERLSR QAAAAEKYKQ YKEEERHKSA QLKALRWQGL
DHQVKQLDHV IGELDVSMEA KVAEQRHVDA EIERLREGHN EAQEHFNQVQ QHFYALGAEV
ARLEQSIQHQ RERHQQLHEE FEQVRASWKE ADEHQRLDGE KLAMLEEQLA ELEPRLEESS
ELQDSATETL TLAEEAMQEW QQEWETFNNR AGESRRQAEV EQSRIQHLEK SIERLRDRMG
RLDKEQESLD SGPLATEMRE FQEQVAELQM QREESEMSSE RLQDEINQLR RQNGDRGREL
DDARERLQTL RGRHTSLEAL QKAAMGDDGA VSEWLTRHEL DDHPRLADRI NVAEGWEKAV
EAVLGDALQA VAVEGLDQVG DWLADLTHGR VAMVQPGSDG AGGHSGKTGT PLRDKVSGKA
PEGLLAGVYA VEDLPGALSL RGQLSPGESV VTRDGIWLGP DWLRVVREQD QEAGILERRR
QLEALEEQIE TLTATVEDLK ARLEENREQV AALEEEREET QRQGSRLSRE LGEVNAQVSA
RQVRLEQITM RQERLGRELE ETRGQLEQEQ EQIKEARTVL AEALDAMEQD SGEREALLSR
RDDYRLRLDE ARQQARQHRD QAHQLAMEAQ GARTQADALR QNLARLEGQV ASLAERKALL
ESQLSEGGDD LGLELQQQLD EKLELRLEAE QKLADARRKL EDVEHQMRDL EGRRGQFERQ
AQEVRDAIGQ KRMLWQELST RRQTVAEQLS EQHFDLETVL ANLPEDADEQ AWNQDLEQIA
QRIARLGQIN LAAIDEYQQQ SERKQYLDRQ NEDLEDALRT LDNAIRKIDR ETRTRFKEYF
DRINKGLQAL FPKVFGGGHA YLELTGEDLL DTGVAIMARP PGKRNSTIHL LSGGEKALTA
LSLVFSIFEL NPAPFCLLDE VDAPLDDANV GRFCNLVQEM SSRVQFIYIT HNKIAMEMAH
ALMGVTMHEP GTSRLVSVDV EEAAEMAAM
//
