ID C6WVP2_METML Unreviewed; 1182 AA.
AC C6WVP2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=Mmol_1083 {ECO:0000313|EMBL:ACT47991.1};
OS Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylotenera.
OX NCBI_TaxID=583345 {ECO:0000313|EMBL:ACT47991.1, ECO:0000313|Proteomes:UP000002742};
RN [1] {ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M., Chistoserdova L.;
RT "Complete sequence of Methylotenera mobilis JLW8.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACT47991.1, ECO:0000313|Proteomes:UP000002742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540
RC {ECO:0000313|Proteomes:UP000002742};
RX PubMed=21622745; DOI=10.1128/JB.00404-11;
RA Lapidus A., Clum A., Labutti K., Kaluzhnaya M.G., Lim S., Beck D.A.,
RA Glavina Del Rio T., Nolan M., Mavromatis K., Huntemann M., Lucas S.,
RA Lidstrom M.E., Ivanova N., Chistoserdova L.;
RT "Genomes of three methylotrophs from a single niche uncover genetic and
RT metabolic divergence of Methylophilaceae.";
RL J. Bacteriol. 193:3757-3764(2011).
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. SMC3 subfamily.
CC {ECO:0000256|ARBA:ARBA00005917}.
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DR EMBL; CP001672; ACT47991.1; -; Genomic_DNA.
DR RefSeq; WP_015832026.1; NC_012968.1.
DR AlphaFoldDB; C6WVP2; -.
DR STRING; 583345.Mmol_1083; -.
DR KEGG; mmb:Mmol_1083; -.
DR eggNOG; COG1196; Bacteria.
DR HOGENOM; CLU_001042_2_2_4; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000002742; 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; IPR010935; SMC_hinge.
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; PF06470; SMC_hinge; 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:UP000002742}.
FT DOMAIN 3..1164
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT DOMAIN 529..629
FT /note="SMC hinge"
FT /evidence="ECO:0000259|Pfam:PF06470"
FT COILED 170..211
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 258..334
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 405..492
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 672..790
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 880..914
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 1182 AA; 131826 MW; A479992767D7A554 CRC64;
MRLTHLKLSG FKSFVDPTTL HIHGQRVGVV GPNGCGKSNV MESVRWVLGE SSAKEMRADA
MDAVIFNGSG NRKPISRASV ELVFDNSLGS AAGEWSQYAE ISVKRVIERD KGSTYYINNS
VVRRRDVADL FLGTGLGGRA YAIIGQNTIS RIVEARPEEM RVFLEEAAGV SKYKERRKET
EQRLRDTREN LLRVEDILRE LDTQIVRLQS QAVVAAQYNQ MQQALNMTKA QIWLLKKRDA
SAQWEKSQRA VEALVNALEA QMASLRHSEN TLETLKQQHV ASSEAVNAAQ AAYYEANAEV
SNLENQVQNT ADARDRLQIQ LHQLSVQLEK NAQQRSLVDS AYALAQAELV QANAGFTHAE
DELSAARTAV PVLLQTFQAA LAAFNTSQST WLNTEQRLRL EQANMTHLSR SITETNEQLK
RLQQSYAALQ IPADSLLIEK QSELDALELQ VAELEQHSAH AAQQEQALHA EIKNQRDEVH
QQQRALHVLE AEVNSLAKLQ QSMHKVDDAS ALSAWLTGAG LNNEQQNMRL WQLLRIKSGW
ESAFEAFLGA KLNAIACDQS LLATGVEERA PVAITLATAF AVEEAASNLS TSFTTMLSLV
EHIEPSYRAV LQGWLAGVYV LDAGADATQA MLALQPGECL VNQHGDIYTA HSVTYFGEQS
GLHGVLERQT RLTSLQNQLP EAQAQLALKN EQLVQLEHSM QQLRAAQHTQ QQQLKHVTQQ
AHQLNLSLQQ LKQQQANAIQ RQSMLQADCN LAEEKLQQLQ VESAQKQTVL NALTENLAAL
QQEKVSLEAS KKLADKHLSE ARSQLQLTER LHQEKGFDVK LISNKINELK SKSKSVLEEE
SSLKLRSAEV EATLAAIKME ALRTNLDAAL NIKQQRESSL VSLRNTMVEN EAILQQQERE
RLQHEQQLHP LRDKLEASRL SEQEARIHFE QCQEGLEASD IEEDVLESHL KQSAGTEVKV
TDLERKKTKL VSDIEGLGAV NLAAIEELAS EQSRKQYIDS QCQDLTEASK TLEDAIYKID
RETRSRLQHT FDEANKHFNE LFTTLFGGGQ AKLEMLGDEI LDTGMQVFAQ PPGKKNSTIH
LLSGGEKALT ALALVFALFR LNPAPFCLMD EVDAPLDDSN TERFCAMVQK MSEKTQFLYV
SHNKITMEMA QQLIGVTMQE SGVSRIVDVD MEAAVKMVEI AS
//
