ID A0A074MDZ7_9SPHN Unreviewed; 1140 AA.
AC A0A074MDZ7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=EH32_12575 {ECO:0000313|EMBL:KEO93056.1};
OS Erythrobacter litoralis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO93056.1, ECO:0000313|Proteomes:UP000027866};
RN [1] {ECO:0000313|EMBL:KEO93056.1, ECO:0000313|Proteomes:UP000027866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO93056.1,
RC ECO:0000313|Proteomes:UP000027866};
RA Zheng Q.;
RT "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
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. {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:KEO93056.1}.
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DR EMBL; JMIX01000007; KEO93056.1; -; Genomic_DNA.
DR RefSeq; WP_034903901.1; NZ_JMIX01000007.1.
DR AlphaFoldDB; A0A074MDZ7; -.
DR KEGG; elq:Ga0102493_112060; -.
DR PATRIC; fig|39960.10.peg.1149; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000027866; 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; 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 PANTHER; PTHR43977:SF2; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1.
DR PANTHER; PTHR43977; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000027866}.
FT DOMAIN 3..1124
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 875..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 161..209
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 235..499
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 613..758
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 787..856
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COMPBIAS 875..891
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 1140 AA; 123214 MW; 2BF7384C45975B96 CRC64;
MQISRLKLSG FKSFVEPAEL RIEPGLTGVV GPNGCGKSNL LEAIRWVMGE NSPKSMRSGG
MEDVIFAGTS TRPPRAFAEV VLHAHDEDGE DLVVTRRIER GAGSAYRVNG RDVRAKDVAL
TFADAATGAH SPALVSQGKI AQVIAAKPAE RRAMLEEAAG IAGLHVRRKD AESKLRQTEA
NLARLEDLMA GLDAQMNSLR RQAKQAERYK ALTDEIGTAE ARLLFARWRD AARSAKEARA
AAEGAEARVA EAQAKVAEAQ KEQAAAAKTL AAARDELADR RDDASAHGHR MAALSEKLEA
AEARLSDLTR QRERLEADRE DADRLTTDAV DALSRLSREL EASRKAVEEA EKERPALADA
AEKAERASRA AELALAKATA DHAGVEAEWR VAEAAIEQAE ARLSRLTAER ERLERTRAEL
EEAQDTEAAV IAAREAAQEA AGDVARLRER LETEQARKAE LQSARDEASA QLAGAKAELA
GIEREYNALA RDRDAREKRE KGRHGLPAAL DRVSVAKGYE RALAAVLGRD AKSPLGAPEA
GAEGRFWSGS ETPRELPDSL LAHVTDCPAE LRARLALVHV AEEDDGRDLA PGEWLVTSAG
HLRRWDGFLA RGEGSAEAAR LEAANRLAEL EEQLPALRAA AGNAATSETA AREELSALQT
ALVALERELA GTVETERQAW RALDQAEAAR ERIAARLAEL SDSEDDLAEQ LSAATSDLEA
AKAKRAELPA PDAGRAALEA AQAKNEAARS AVQATLAELA SHDQSLAVAR ERLAAQKSDH
AGWQARSSDA ERRMSEAASR LEEIEEERAI HAAKPAALMA EIEQGDTLRE RLAKELAEAE
QTMQLAQDAL GDVERVLAEA TETLAQAREG RATLAARAEN EESRRSEMAR VSGERFQCPP
PLLSERFAFA EDEVKPASEE SEALDRLTAS RERIGPVNLV AADELARIEE EHGTNASEQA
ELAEAVARLR GSIGNLNREG RERLRAAFEE VDGHFRVLFT RLFQGGQAHL ALVDSDDPLE
AGLEIYAQPP GKRLQSLSLL SGGEQALTAT ALIFALFLTN PAPICVLDEV DAPLDDANVE
RFCDLLDSMV RTTSTRYLIV THNAVTMSRM HRLFGVTMAE KGISRLVSVD LGEAELMAAE
//
