ID A0A0H0XUR8_9SPHN Unreviewed; 1138 AA.
AC A0A0H0XUR8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AAV99_06800 {ECO:0000313|EMBL:KLI64040.1};
OS Aurantiacibacter marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI64040.1, ECO:0000313|Proteomes:UP000053455};
RN [1] {ECO:0000313|EMBL:KLI64040.1, ECO:0000313|Proteomes:UP000053455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI64040.1,
RC ECO:0000313|Proteomes:UP000053455};
RA Zhuang L., Liu Y., Shao Z.;
RT "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL Submitted (APR-2015) 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:KLI64040.1}.
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DR EMBL; LBHU01000002; KLI64040.1; -; Genomic_DNA.
DR RefSeq; WP_047093291.1; NZ_LDCP01000002.1.
DR AlphaFoldDB; A0A0H0XUR8; -.
DR STRING; 874156.GCA_001021555_01960; -.
DR PATRIC; fig|874156.12.peg.1400; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000053455; 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; 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 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:UP000053455}.
FT DOMAIN 4..1122
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 168..222
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 252..328
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 458..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 618..701
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 827..882
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 1138 AA; 123452 MW; 3FAF647DED842551 CRC64;
MEFRKLRLSG FKSFVEPSEL RIEPGLTGVV GPNGCGKSNL LEAIRWVMGE NSPKSMRSGG
MEDVIFAGTS TRPPRDFAEV VLHAVDDGGE DLDVTRRIER GAGSAYRMNG SDVRAKDVSL
IFADAATGAH SPALVSQGKI AQVIAAKPTE RRMMLEEAAG IAGLHVRRRD AELKLRSTEK
NLERLEDLMA GLDTQMNSLR RQAKQAERYK KLSDEIRIAE ARLLFARWRD AAAAAEAARS
QAKAADDKVT GAQAVAKEAQ KAQAALAEKL AELRDELADR RDDTSAHGHR MAALASQLEA
AQQRLSDLDR QKERLEEDKF EADRMTQDAA KALKDLEAAL GAGETALQAD EAKRPDLVEK
VEDSERAGRN AELALAKATA DHAGVEADWR VAQSEIAQAE ARLARLAGEA QRIAAQREDL
TGARDPQEAL AEAREAATAA TALVTLRQKE LESDRTAKES ITQARDDARE AFASAKAELA
GTEREYAALE RDRAARAKQQ ANRSGRALPI DQVRAAPGYE RALAAALGRD AKSPLGTPEG
EGRFWTGRAA PAPVADSLAN HITNCPEELA ARMALVHVAD ADDGRTLEPG HWIVTRAGAL
RRWDGFVAHG EGGAEAARLE AENRFAELAE KLPALQSRMR DTEAQVAETQ DRYARLQQAI
IERDRSIAQA IEAERAALRS VDQAEAAVAQ MASRLEQIEA ATAELSGQQE AATADLDTAK
ARLAELPDPE TGRASLDAAR ARHEAARESL QAATASLAAH DQSLAVLRER VATQRADMQG
WQARAGDAAN RLAGMSARFE EIEEERAVVA AKPEGLMREI ESGEAVRKRL GEELATAEAA
VRETEAQARE ADAALGDLTE ALAAAREQRA TLATRAENEE QRREEMARIS GERFQCPPSL
LPGRFEFDEE EVKNSGLESD DMDRLVASRE RIGPVNLVAA DELEKMESEH GSSAAEQAEL
AEAVNRLRGS IGNLNREGRE RLKAAFEEVD GHFRRLFTRL FEGGQAHLAL VDSDDPLEAG
LEIYAQPPGK RLQSLSLLSG GEQALTATAL IFALFLTNPA PICVLDEVDA PLDDANIERF
CDLLDSMVRE ANTRYLIVTH NAVTMSRMHR LFGVTMVEKG ISRLVSVDLG EAAALAAE
//
