ID K9S574_9CYAN Unreviewed; 558 AA.
AC K9S574;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=GEI7407_0413 {ECO:0000313|EMBL:AFY64914.1};
OS Geitlerinema sp. PCC 7407.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC Geitlerinemataceae; Geitlerinema.
OX NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY64914.1, ECO:0000313|Proteomes:UP000010383};
RN [1] {ECO:0000313|EMBL:AFY64914.1, ECO:0000313|Proteomes:UP000010383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY64914.1,
RC ECO:0000313|Proteomes:UP000010383};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Geitlerinema sp. PCC 7407.";
RL Submitted (MAY-2012) 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}.
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DR EMBL; CP003591; AFY64914.1; -; Genomic_DNA.
DR RefSeq; WP_015170482.1; NC_019703.1.
DR AlphaFoldDB; K9S574; -.
DR STRING; 1173025.GEI7407_0413; -.
DR KEGG; gei:GEI7407_0413; -.
DR PATRIC; fig|1173025.3.peg.459; -.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_019008_0_0_3; -.
DR OrthoDB; 9803036at2; -.
DR Proteomes; UP000010383; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 Lyase {ECO:0000313|EMBL:AFY64914.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037250-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000010383};
KW Zinc {ECO:0000256|PIRSR:PIRSR037250-51}.
FT DOMAIN 223..316
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT DOMAIN 344..436
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT DOMAIN 461..556
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT REGION 312..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-50"
FT BINDING 75
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 102
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 107
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 194..200
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-52"
SQ SEQUENCE 558 AA; 60084 MW; C07FBB0BA53C8749 CRC64;
MAVHSFAAPP TPWSQDLAEP QVHDTAYVHA FSNIIGDVRV GPNVLVAPGT SIRADEGSPF
FIGANTNIQD GVVVHGLEQG RVLGDDQEPY SVWIGSNASI THKALIHGPA YIGDDCFIGF
RSTVFNARVG KGCIVMMHAL IQDVEIPPGK YVPSGAVITS QQQADRLPDV QDEDREFARH
VVGINEALRS GYQCAEDSVC IAGIRNEAPK TKETDGVNGF SRLSGQMQST QLSSETLDQV
RHLLNSGYRV GTEHADTRRF QTSSWHSCAP IQSSRESEVV GALEACLREH EGEYVRLIGI
DTRSKRRVLE SIIQRPGDRS GQASRPTTTS SYSGGNGNGA AASRGAAVAP SANADVADLV
RQLVAQGCRV SLEHADERRF KTSSWRSGPL MQTSQASEVI AVVQSFLAEH RNEYVRLVGI
DSAAKRRVVE VTIQRPGESA NVASGAGSSS YSAPSAPSYS SSSNSSATSG RLAPEIVDQL
RQLLAQGCRI GVEHADARRY RTSSWHSCPA IDSTQLQTVV GILERCVADH PGEYVRLIGI
DPKAKRRVAE TLIQRPGQ
//
