ID Q9K0P1_NEIMB Unreviewed; 1161 AA.
AC Q9K0P1;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN OrderedLocusNames=NMB0545 {ECO:0000313|EMBL:AAF40974.1};
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF40974.1, ECO:0000313|Proteomes:UP000000425};
RN [1] {ECO:0000313|EMBL:AAF40974.1, ECO:0000313|Proteomes:UP000000425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58 {ECO:0000313|EMBL:AAF40974.1,
RC ECO:0000313|Proteomes:UP000000425};
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L.,
RA White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A.,
RA Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H., Qin H., Vamathevan J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF40974.1; -; Genomic_DNA.
DR PIR; G81186; G81186.
DR RefSeq; NP_273590.1; NC_003112.2.
DR RefSeq; WP_002225580.1; NC_003112.2.
DR AlphaFoldDB; Q9K0P1; -.
DR STRING; 122586.NMB0545; -.
DR PaxDb; 122586-NMB0545; -.
DR KEGG; nme:NMB0545; -.
DR PATRIC; fig|122586.8.peg.693; -.
DR HOGENOM; CLU_001042_2_2_4; -.
DR InParanoid; Q9K0P1; -.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000000425; 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; 2.
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:UP000000425}.
FT DOMAIN 3..1144
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..485
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01894"
FT COILED 671..879
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 1161 AA; 130410 MW; 21764D8C55C6066B CRC64;
MRLTHIKLSG FKSFTDPTTI HVPGQLVAVI GPNGCGKSNV IDAVRWVLGE ASAKQLRGES
MQDVIFNGAA TRRPAPRASV ELVFDNSDHS LQGAWGQYAE VSIKRQLTRQ GESTYFINNQ
TVRRRDITDL FLGTGVGARG YAVIEQGMIS RIIEARPEEL RAYIEEAAGV SKYKERRKET
EGRLKDTREH LQRLGDLQNE LARQVEKLEK QAETAERYKS LTAQLNQQQD LLDYAQWRQS
LAAADKATAQ HQSLQAQQDE TAAQVQALND EVHALQTAEQ SQQQAVHELS NKRGVLREQI
ARLEEQIRHQ QNLHQRIERD KQAAQAQLQR IHQEQQQIRV QLEENELQVE EKQTELAEWA
MQVAEHEERL PELEEAQATL NAAFQTQQDE ANRIRRELAL KQQQLAHAEQ TIAKHEERKG
RLKQENQALN LPDEAETAAA QEAAALLQSQ QEHYEEQIIA AEEALHAARE AFQTASNRFQ
SLKQQHITLQ AQQQALSQIL SQQQEAADFW QATDHAAAPQ LWQHITAPAE WQHALSVILA
ERLHARAVPQ GFVPPEPLPQ GQAAWLSDDL SGGIKKSLPV QALLNQIQAQ PPFQTALHYW
LDGVLCAPDL SYALAHQNDL GAHQIWLTPE GHQVDKVSVL LYAKPAQESL IAQKARLDGI
ASELENLAPE LSAAEAAFKQ AEAAVRSSEV QHKNLMQQQQ QHTRQYSQAQ QRAAELLART
NQGQIRREHI ERELAQLAEE QTVLQHTSDG LSDDIVTLQE AAAELEHQQQ TTAHSRQEQQ
GRLKQAQLAL LEANRQYGLA EVAVHKLNQQ KQNYRQQIAQ LEQQTLDWQE RQQELALAYE
TEFQNDEQHI KLEELSEAVQ TLDEEYIVVQ EKLAQIQEQG REQYAKVQTL QTKLPQLQAA
TQTALLQQQE ALINAKRYHQ NLTERAADLD ALEALAKESP KVLNSSIGSL SQQIEALGAV
NLAALQELEE ARERDGYYRS QSEDVQAAIT LLEEAIAQID DKTKARFKET FDAVNSKVQT
FFPTLFGGGE ATLKMIGDDL LTAGVSIMAR PPGKKNSTIH LLSGGEKALT AMSLVFALFS
LNPAPFCLLD EVDAPLDDAN TSRFCRLVKE MSAQTQFLYI SHNRLTMEMA EQLVGVTMQE
KGVSRVVAVD IKQALEMAEA V
//
