ID A0A095VPM0_9GAMM Unreviewed; 1165 AA.
AC A0A095VPM0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=HRUBRA_01796 {ECO:0000313|EMBL:KGE03417.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE03417.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE03417.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE03417.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(2014).
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:KGE03417.1}.
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DR EMBL; AUVB01000054; KGE03417.1; -; Genomic_DNA.
DR RefSeq; WP_035513307.1; NZ_KN234745.1.
DR AlphaFoldDB; A0A095VPM0; -.
DR STRING; 1265313.HRUBRA_01796; -.
DR PATRIC; fig|1265313.6.peg.1775; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_6; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000029640; 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; 1.
DR SUPFAM; SSF57997; Tropomyosin; 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:UP000029640}.
FT DOMAIN 3..1149
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..231
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 300..425
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 659..763
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 806..882
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 980..1007
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 1165 AA; 128464 MW; 597621F6E24A10EF CRC64;
MRLKSIKLSG FKSFVDATTV TFPSNMAAVV GPNGCGKSNI IDAVRWVMGE SSAKNLRGES
MADVIFNGSV NRQPVGQASI ELIFDNSDGG VGGEYASYAE IATRRQVSRE GQSEYFLNGT
RCRRRDITDI FLGTGLGPRS YAIIEQGMIS RLIESRPEEL RIFIEEAAGI SKYKERRKET
ESRMRRTLEN LERLTDIRDE LERQLQHLQR QAQAAERYSA LKEEERTLKA QLLALEWKEL
DSEAAASAHK VGELEVSLEA VLAEHQQVDT RIEQQRVEQT ERSDVFNEVQ GRYYTLGAEV
ARIEQSIQHQ KERSRQLRED LAQTRSNLEE AQRHLREDRE RLETWDEELA GLAPESEVLD
AAAEEAATAL AAAEEAMQGW QQRWDEFNHR AAEPRQQAEV QQSRIQHLEH ALKRLQARIE
LLAREQQELA PAAGEEDPAP LREELADAEL AIAGYEEQGE AVAADLAVSR EEGTRLAREL
DAARSQLAQL RGRQSSLEAL QQAAAEDAAG GADDWLSGNG LATAPRLLSQ LEVAAPWQRA
VETVLGDYLH AVCVDDLDGL GQRLDGLAAG HLTLVARGAA TPASGGTLAA QVRCGGRVAG
LLAAVRTAAD ESEALALRGE LAGHESVITP EGLWLGPNWL SLRRGEAEAG GVIRRQQELE
ELSLAVEETG ARVRQLEELQ AGEAQRLRDL ESARQALQRD QQAASRRQAD AAARLKAQEA
RVEQLDARRA ALARDAADAR GQFESEQASI AEARQVLAEA IERMEADAGE RESLLSERDR
LRGGLDGCRQ AARQARDGAH QAAMRLRSLQ TQVETIRSSI DRSQAQVAQL SERQETLASG
LEDSSTPVAE LEAELETQLQ LRAAAEVELT GARQRVAEIE HALRSDEQAR SGVEQRIAAA
RAELEQCRLG RQTLEVQREN VGRQLKELAQ DPEAVLEGLP EDATRDGWQQ QLERVAARIA
RLGPINLAAI DEYSQQSERK QYLDAQNEDL ESALATLESA IRKIDRETRS RFQVTFDKVN
SGLQELFPRV FGGGNAYLEM TGDDLLDTGI SIMARPPGKK NSTIHLLSGG EKALTAIALV
FSIFQLNPAP FCMLDEVDAP LDDANVGRYA RMVKEMSGKV QFIFITHNKI TMEMADQLLG
VTMHEPGVSR LVAVDVEEAA ELAAS
//
