ID V4NNG4_9CAUL Unreviewed; 1157 AA.
AC V4NNG4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN ORFNames=AEAC466_14050 {ECO:0000313|EMBL:ESQ83367.1};
OS Asticcacaulis sp. AC466.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ83367.1, ECO:0000313|Proteomes:UP000017826};
RN [1] {ECO:0000313|EMBL:ESQ83367.1, ECO:0000313|Proteomes:UP000017826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC466 {ECO:0000313|EMBL:ESQ83367.1,
RC ECO:0000313|Proteomes:UP000017826};
RX PubMed=24463524; DOI=10.1038/nature12900;
RA Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT "Sequential evolution of bacterial morphology by co-option of a
RT developmental regulator.";
RL Nature 506:489-493(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:ESQ83367.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWGE01000013; ESQ83367.1; -; Genomic_DNA.
DR RefSeq; WP_023458804.1; NZ_AWGE01000013.1.
DR AlphaFoldDB; V4NNG4; -.
DR STRING; 1282362.AEAC466_14050; -.
DR PATRIC; fig|1282362.3.peg.2773; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000017826; Unassembled WGS sequence.
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 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; 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:UP000017826}.
FT DOMAIN 4..1138
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 177..214
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 300..327
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 703..771
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 835..890
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 938..993
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 1157 AA; 126610 MW; 3265095F2097212D CRC64;
MQFQKIKLSG FKSFVDATEF RIDPGLTGIV GPNGCGKSNL LEALRWVMGA TSAKAMRGAG
MDDVIFAGSD KRPSRNWAEV TLTIDNAERL APQPFTDQPV LDVARRIDRG AGSSYRINGK
EVRARDVQLL FADASTGANS PALVRQGQIS ELIAAKPQNR RRVLEEAGGV SGLHTRRHEA
ELRLSAAEQN LSRLDDIARE LDSALSRLKR EARQADKYKK ISAEIRALQK AILHAKWLEV
RALLEGAVSD MQAQSARVEA TTRAASVGQT AALKAAELIP PLREEEAVAA TVNHRLNIEK
ERLDLEEKQA ASEIERLKGD IARLRADFQR EVDLSSDGSV QVERLQSGLA RVQEEIAAAP
SREPELKAAV EAAEAERGKA DHAIEIVAAE QAAVVERARL EAARLTEAKS RFDRLNTQLQ
TAQNDRKALG TFDYGAVEGL KAQAMQAQAD LDAGRKAVED LDAGRVALIN AEAQARKTAR
DIEDQLGRLT AEARGLSQIL AGNRKDGVPV LDQVRPDKGY ELALAAALGD DLNLSLSKKD
VQSALAFWSE DFESRAQRID MAALGVTPLS DHVRAPDALS LRLSTVGIVS RDDGDRLQSL
LPIGGRLVSR EGDLWRWDGL IVRAKAPKPA AVRLAQRTRH DELETEIDGL KPRLVAAQSA
QADAANAQRS HEDALRTARN RLPDLERAVR SRQTALDERL RAQTQFEARL EGLEATLARL
TGEQAEAKAA YDTLVAAQSD ALDTEGMKAR MNAARAEADT YRQAVMKARA DLDQDIRDRQ
AREGRERTLT RELTEWSRRT QDSAARLLKL ERDQETARVA LETAQSAPRK FESKRIALID
SLQTAEKRLN EARDKLNAAE AERRDADINV RILEQEASAA REERAGATAR LEAIQGKAGE
IEAMILDQTG GSPDDLGKRL KEEAIATPTD ASGAESLLSG LERERDQLGA VNLRAEEEAT
EYEGRLDTLS RERSDLTTAI AKLRDGIDEL NAEGRERLLA AFEIINEHFK TLFVTLFDGG
SAELRLVESD DPLEAGLEIF ACPPGKRLST MSLMSGGEQA LTATALIFGV FLANPAPVCV
LDEVDAPLDD ANVDRYCRLL AEMRGRTKTR FIAITHNPVT MSRMDRLFGV TMSERGVSQL
VSVDLSQAEA LVAENVA
//
