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Database: UniProt
Entry: A0A0F5YGQ4_9CYAN
LinkDB: A0A0F5YGQ4_9CYAN
Original site: A0A0F5YGQ4_9CYAN 
ID   A0A0F5YGQ4_9CYAN        Unreviewed;       551 AA.
AC   A0A0F5YGQ4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=WN50_10970 {ECO:0000313|EMBL:KKD38046.1};
OS   Limnoraphis robusta CS-951.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Sirenicapillariaceae; Limnoraphis.
OX   NCBI_TaxID=1637645 {ECO:0000313|EMBL:KKD38046.1, ECO:0000313|Proteomes:UP000033607};
RN   [1] {ECO:0000313|EMBL:KKD38046.1, ECO:0000313|Proteomes:UP000033607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CS-951 {ECO:0000313|EMBL:KKD38046.1,
RC   ECO:0000313|Proteomes:UP000033607};
RA   Willis A., Parks M., Burford M.A.;
RT   "Draft genome assembly of filamentous brackish cyanobacterium Limnoraphis
RT   robusta strain CS-951.";
RL   Submitted (JUN-2015) 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:KKD38046.1}.
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DR   EMBL; LATL02000220; KKD38046.1; -; Genomic_DNA.
DR   RefSeq; WP_046278582.1; NZ_LATL02000220.1.
DR   AlphaFoldDB; A0A0F5YGQ4; -.
DR   PATRIC; fig|1637645.4.peg.4340; -.
DR   OrthoDB; 9803036at2; -.
DR   Proteomes; UP000033607; 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; 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; PF14602; Hexapep_2; 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:UP000033607};
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          340..431
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   REGION          430..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..465
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   551 AA;  59153 MW;  252C45978590904B CRC64;
     MAVRSIAAPP TPWSKNLAEP KIDSTAYVHS FSNIIGDVRI GANVLVAPGT SIRADEGFPF
     YIGENSNIQD GVVIHGLEEG RVKGDDGQSY SVWIGKNTSI THMSLIHGPA YVGNNCFIGF
     RSTVFNARVG DGCIIMMHTL IQDVEIPSGK YVPSGAIITN QQQADRLPDV NDADLKFSTH
     VIGVNQALKA GYKCSENAAC LTGIRNEVSP SASNGGGRDR SYAYASSGSL DASIVAQVNQ
     LLAQGYKIGS EHADKRRFRT SSWRSCTPID SNNSKDVMAA LEACLQEHQG EYVRLLGIDP
     QAKRRVFEEI IQRPDGIVQK SSNAQVSAPA FRASAPSPAS ASVASSMSSS LSEQISQLLA
     QGCKIGLESA DKRRFRTSSW NSGPSIESTR VADVVAQVEA FVSEHSGEYV RLIGIDPKAK
     RRVVEEIIQR PDGPAPSAPQ STIAPTARPV ASQPAASVSS SNGGGVNSEL ITSVRSLLAQ
     GYKIGTEHAD KRRFRTGSWH SCAPIESTRD SEVIAALEGC MKEHSGEYVR MIGIDPKAKR
     RVMEEIIQKP N
//
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