ID D0W2R4_NEICI Unreviewed; 1161 AA.
AC D0W2R4;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Chromosome partition protein Smc {ECO:0000256|HAMAP-Rule:MF_01894};
GN Name=smc {ECO:0000256|HAMAP-Rule:MF_01894,
GN ECO:0000313|EMBL:EEZ71712.1};
GN ORFNames=NEICINOT_03949 {ECO:0000313|EMBL:EEZ71712.1};
OS Neisseria cinerea ATCC 14685.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546262 {ECO:0000313|EMBL:EEZ71712.1, ECO:0000313|Proteomes:UP000003294};
RN [1] {ECO:0000313|EMBL:EEZ71712.1, ECO:0000313|Proteomes:UP000003294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14685 {ECO:0000313|EMBL:EEZ71712.1,
RC ECO:0000313|Proteomes:UP000003294};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2009) 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}.
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:EEZ71712.1}.
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DR EMBL; ACDY02000005; EEZ71712.1; -; Genomic_DNA.
DR RefSeq; WP_003676266.1; NZ_ACDY02000005.1.
DR AlphaFoldDB; D0W2R4; -.
DR STRING; 546262.NEICINOT_03949; -.
DR eggNOG; COG1196; Bacteria.
DR OrthoDB; 9808768at2; -.
DR Proteomes; UP000003294; 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; 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; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
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}.
FT DOMAIN 3..1144
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT COILED 170..471
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; 130288 MW; A89F4FE7C13EA30E CRC64;
MRLTHIKLSG FKSFTDPTTI HVPGQLVAVI GPNGCGKSNV IDAVRWVLGE ASAKQLRGES
MQDVIFNGAA TRRPAPRASV ELVFDNSDHS LQGAWGQYAE VSIKRQLTRQ GESTYFINNQ
TVRRRDITDL FLGTGVGARG YAVIEQGMIS RIIEARPEEL RAYIEEAAGV SKYKERRKET
EGRLKDTREH LQRLGDLQNE LARQVEKLEK QAETAERYKS LTAQLNQQQD LLDYAQWQQS
LAAADKATAQ HQSLQAQQDE TAAQVQALND EVHALQTAEQ SQQQAVHELS NKRGVLREQI
ARLEEQIRHQ QNLHQRIERD KQAAQAQLQR IYQEQQQIRV QLEENELQAE EKQTELAEWA
MQVAEHEERL PELEEAQATL NAAFQTQQDE ANRIRRELAL KQQQLAHAEQ TVAKHEERKG
RLKQENQALN LPNEAETAAA QEAAALLQSQ QEHYEEQIIA AEEALHAARE AFQTASNSFQ
SLKQQHITLQ AQQQALSQIL SQQQEAADFW QVTDHAAAPQ LWQHITAPAE WQHALSVILA
ERLHARSVPQ GFVPPTPLPQ GQAAWLSDDL SGGIKKSLPV QALLNQIQAQ PPFQTALHHW
LDGVLCAPDL SYALAHQSDL GAHQIWLTPE GHQVDKVSVL LYVKPAQESL IAQKARLDGI
ASELEKLAPE LSAAEATFKQ AEAAVRSSEV QHKNLMQQQQ QHTRQYSQAQ QRAAELLART
NQGQIRREHI ERELAQLAEE QTVLQHTSDG LSDDIATLQE AAAELEHQQQ TTAHSRQEQQ
SRLKQAQLAL LEANRQYGLA EVAVHKLNQQ KQNYQQQIAR LEQQTLDWQE RQQELALAYE
TEFQNDEQHT KLDELTEAVH TLDEEYIAVQ EKLAQIQEQG REQYARVQSL QTKLPQLQAA
TQTALLQQQE ALINAKRYHQ NLTERAADLD ALEALAKESP KILNSSIGSL TQQIEALGAV
NLAALQELEE ARERDGYYRS QSEDVQAAIT LLEEAIAQID DKTKARFKET FDAVNGKVQT
FFPTLFGGGE ATLKMIGDDL LTAGVSIMAR PPGKKNSTIH LLSGGEKALT AMSLVFALFS
LNPAPFCLLD EVDAPLDDAN TSRFCNLVKE MSAQTQFLYI SHNRLTMEMA EQLVGVTMQE
KGVSRVVAVD IKQALEMAES V
//
