ID K9PDK6_9CYAN Unreviewed; 550 AA.
AC K9PDK6;
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=Cal7507_0757 {ECO:0000313|EMBL:AFY31243.1};
OS Calothrix sp. PCC 7507.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY31243.1, ECO:0000313|Proteomes:UP000010390};
RN [1] {ECO:0000313|EMBL:AFY31243.1, ECO:0000313|Proteomes:UP000010390}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY31243.1,
RC ECO:0000313|Proteomes:UP000010390};
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., Teshima H., Chen A.,
RA Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA Woyke T., Kerfeld C.;
RT "Finished genome of Calothrix sp. PCC 7507.";
RL Submitted (APR-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; CP003943; AFY31243.1; -; Genomic_DNA.
DR RefSeq; WP_015127068.1; NC_019682.1.
DR AlphaFoldDB; K9PDK6; -.
DR STRING; 99598.Cal7507_0757; -.
DR KEGG; calo:Cal7507_0757; -.
DR PATRIC; fig|99598.3.peg.838; -.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG4451; Bacteria.
DR HOGENOM; CLU_019008_0_0_3; -.
DR OrthoDB; 9803036at2; -.
DR Proteomes; UP000010390; 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; IPR001451; Hexapep.
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; PF00132; Hexapep; 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:AFY31243.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037250-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000010390};
KW Zinc {ECO:0000256|PIRSR:PIRSR037250-51}.
FT DOMAIN 225..316
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT DOMAIN 345..437
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT DOMAIN 458..550
FT /note="Ribulose bisphosphate carboxylase small subunit"
FT /evidence="ECO:0000259|SMART:SM00961"
FT REGION 320..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..354
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"
FT DISULFID 269..287
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-53"
FT DISULFID 389..407
FT /evidence="ECO:0000256|PIRSR:PIRSR037250-53"
SQ SEQUENCE 550 AA; 59907 MW; 45C826ABBEDD4C64 CRC64;
MAVRSTAAPP TPWSRSLAEP QIHETSFVHS FSNLIGDVRI GANVIVAPGT TIRADEGTPF
YLGENTNIQD GVVIHGLEQG RVIGDDQNQY SVWIGKNTCI THMALIHGPA YVGDNSFIGF
RSTVFNARVG AGCIVMMHAL IQDVEIPPGK YVPSGAIITN QQQADRLPDV QEQDEEFAHH
VVGINQALRA GYRCAADSKC IAPIRDENTK SYTSNGVTVL ELERSSEVSS NRLGAETIEQ
IRYLLEQGYK IGTEHVDQRR FRTGSWTSCQ PIEPRSIGEA IAALESCLRD HSGEYVRLFG
IDKGRRRVLE TIIQRPDGTV GAPANFRAPA TQSHHSYNGG GNGSSNGNGS GRISSETVDQ
IRQLLAGGYK IGTEHVDERR FRTGSWQSCE AINANSANDV VAALEDCINN HQGEYVRLIG
IDTKAKRRVL ESIIQRPNGQ ASPSGSQKSF VSTTATATAT ATSTRLSTEV VDQLRQLLAG
GYKISVEHVD QRRFRTGSWT STGPIEATSE RAAIAALEAN LAEYPGEYVR LIGIDSKAKR
RVLETIIQRP
//
