ID M1X366_9NOST Unreviewed; 550 AA.
AC M1X366;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Carboxysome assembly protein CcmM {ECO:0000256|ARBA:ARBA00023636};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmM {ECO:0000256|ARBA:ARBA00030397};
GN ORFNames=RINTHH_18850 {ECO:0000313|EMBL:CCH68040.1};
OS Richelia intracellularis HH01.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Richelia.
OX NCBI_TaxID=1165094 {ECO:0000313|EMBL:CCH68040.1, ECO:0000313|Proteomes:UP000053051};
RN [1] {ECO:0000313|EMBL:CCH68040.1, ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|EMBL:CCH68040.1,
RC ECO:0000313|Proteomes:UP000053051};
RA Hilton J.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH01 {ECO:0000313|Proteomes:UP000053051};
RA Hilton J.A., Foster R.A., Tripp H.J., Carter B.J., Zehr J.P.,
RA Villareal T.A.;
RT "Diatom-associated endosymboitic cyanobacterium lacks core nitrogen
RT metabolism enzymes.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000256|ARBA:ARBA00023587}.
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000256|ARBA:ARBA00023595}.
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:CCH68040.1}.
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DR EMBL; CAIY01000076; CCH68040.1; -; Genomic_DNA.
DR AlphaFoldDB; M1X366; -.
DR STRING; 1165094.RINTHH_18850; -.
DR OrthoDB; 9803036at2; -.
DR Proteomes; UP000053051; Unassembled WGS sequence.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043886; F:structural constituent of carboxysome shell; IEA:InterPro.
DR CDD; cd00710; LbH_gamma_CA; 1.
DR CDD; cd00307; RuBisCO_small_like; 3.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 1.
DR Gene3D; 3.30.190.10; Ribulose bisphosphate carboxylase, small subunit; 3.
DR InterPro; IPR047223; CA_gamma_LbH.
DR InterPro; IPR017156; CcmM.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43360; CARBON DIOXIDE CONCENTRATING MECHANISM PROTEIN CCMM; 1.
DR PANTHER; PTHR43360:SF1; CARBOXYSOME ASSEMBLY PROTEIN CCMM; 1.
DR Pfam; PF00101; RuBisCO_small; 3.
DR PIRSF; PIRSF037250; CcmM; 2.
DR SMART; SM00961; RuBisCO_small; 3.
DR SUPFAM; SSF55239; RuBisCO, small subunit; 3.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 1.
PE 3: Inferred from homology;
KW Bacterial microcompartment {ECO:0000256|ARBA:ARBA00023669};
KW Carboxysome {ECO:0000256|ARBA:ARBA00023669};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037250-52};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037250-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000053051};
KW Zinc {ECO:0000256|PIRSR:PIRSR037250-51}.
FT DOMAIN 221..314
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT DOMAIN 338..433
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT DOMAIN 457..550
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT ACT_SITE 55
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-50"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-51"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-51"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-51"
FT DISULFID 193..199
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-52"
FT DISULFID 266..284
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-53"
FT DISULFID 385..403
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-53"
SQ SEQUENCE 550 AA; 61110 MW; F3C667FBD11D3FCA CRC64;
MVSSTAAPPT PWSRNLAEPQ IHQTAYIHHF SNIIGDVVVS PNVIISPGTS IRADEGTPFY
IGENTNIQDG VVIHGLEQDR VIGDDKRDYS VWIGNNVCIT HMALIHGPAY VGNDCFIGFR
STVFNAKIGA GCIIMMHALI ENVEIPPGKY VPSGAIITTQ QQANRLPDVQ ADDKQFAHHV
VGINQALRAG YLCAQDNQCI APIRDEMNKS HKSTNLNGFE RSNQVSSSKL DTAVVDRVRY
LLQQGYKIAT EHVDERRFRT GSWSSCTPIE ARSLEQVIVS VENCLIDHSG EYVRLFGINT
KERCRILETI IQRPNGTVHE LSTFKLPMPR LPNGEIANNG NTSVSSGLIG KETIETVNQL
LAGGFMIGVE HVDERRFRTG SWQSCQSCDN SSANRVIEFL EECMVNHQGE YVRLIGIDPK
IKRRVLETII QRPNGVIAAS EKNQLSIDQD PHNRVSKYTS VNTNNLGSEV IDKIRQLLAG
GLKISAEHVD KRRFRTGVWS SCGQITSHSE EGIINALGHL MTEYQGEYLR VVGIDTKAKC
RVIERIIQRP
//
