ID A0A0P0NWM4_9CAUL Unreviewed; 1148 AA.
AC A0A0P0NWM4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-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=AQ619_01545 {ECO:0000313|EMBL:ALL12148.1};
OS Caulobacter henricii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=69395 {ECO:0000313|EMBL:ALL12148.1, ECO:0000313|Proteomes:UP000056905};
RN [1] {ECO:0000313|EMBL:ALL12148.1, ECO:0000313|Proteomes:UP000056905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:ALL12148.1,
RC ECO:0000313|Proteomes:UP000056905};
RA Scott D., Ely B.;
RT "Conservation of the essential genome among Caulobacter and Brevundimonas
RT species.";
RL Submitted (OCT-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}.
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DR EMBL; CP013002; ALL12148.1; -; Genomic_DNA.
DR RefSeq; WP_062143292.1; NZ_CP013002.1.
DR AlphaFoldDB; A0A0P0NWM4; -.
DR STRING; 69395.AQ619_01545; -.
DR KEGG; chq:AQ619_01545; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000056905; 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; 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; IPR036277; SMC_hinge_sf.
DR InterPro; IPR011890; SMC_prok.
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; 2.
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:UP000056905}.
FT DOMAIN 4..1131
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 177..221
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 293..320
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 366..478
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 703..730
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 1148 AA; 123408 MW; 8DEB45E4AE644D99 CRC64;
MQFQRLRLSG FKSFVEPTEF RIEPGLTGIV GPNGCGKSNL LEALRWVMGA NSAKAMRAGG
MDEVIFAGSG ARPARNHADV TLTIDNADRT APAQFNDDPV LEVVRRIDRG EGSTYRINGR
EVRARDVQLL FADASTGANS PALVRQGQIS ELIGAKPQNR RRILEEAAGV SGLHTRRHEA
ELRLRAAETN LSRLEDVARE LESALNRLRR EARQAEKYKR LSSEIRAVQG AVLFARWTEA
RDTLNRTQSE ATQAARNVED TARAASSAQV EITRAEAAMP PLREEATIAQ AVLGQLAIQK
DRAEREAEAA AAEFQRLSAD LARIDDDRAR EVQTQQDAAA ALARLDGELA EIRALVAAAP
ERGPELAAAA KAAEEARADA EAVVEQLAAR AAAEDARARA ATARLADAEG RLARTRRALD
QARSERAAVG PETDPAAADA RQRFDNAQTG LNAARAALET AEAERAKAAE QEAMARQLAR
SVEDQLGRLR TEARGLANLT APRSRSGHAP ALDSVSPDKG YGAALAAALG DDLDAALDPR
AASYWGGAGT PSPVWPEGAQ PLAPLVKAPP ELAARLAFTA VVQRGEGDRL QKGLSPGMRL
VSAEGDLWRW DGFVARADAP RPAAVRLEQR TRLAEVEAEI DLTAPRAEAT TGALKIATDR
LRTAEDNLRE RRRAPPEAER LLAGARDAVA QFERTAALRA ARAQSLDETI DRFESEQAEA
EAALAAVRAE HAGATAVADL APQLAEARQA AATAREAASA ARTALDVETR ERAGRQRRLE
ALERDHGDWT RRAETAGKRI AALDADRVKA ASALEAAREA PTVLKDRLLV LLEEFGAAEA
RRIRASDALE TAETARLTAD RAARAAGQAA SEAREARAAL VAHLDGARAR FAEIAGSIRE
SVRMEPEELG RHVAGEAVAV PKDAAGVEAH LFALERERDA IGPVNLRAEE EAQEYAARLE
IMRSERADLS GAVGKLRAGI EELNAEGRER LLAAFEVING HFQTLFQALF GGGQAELRLI
ESDDPLEAGL EIYACPPGKR MASMSLMSGG EQALTASALI FGVFLANPAP ICVLDEVDAP
LDDANVDRYC NMLDEMRRRT QTRFIAITHN PVTMSRMDRL FGVTMGERGV SQLVSVDLNT
AEQMVAAQ
//
