CCMM_SYNY3
ID CCMM_SYNY3 Reviewed; 687 AA.
AC P72758;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Carboxysome assembly protein CcmM {ECO:0000305};
DE Short=CcmM73 {ECO:0000303|PubMed:17993516};
DE Short=M73 {ECO:0000303|PubMed:17993516};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmM;
GN Name=ccmM {ECO:0000303|PubMed:17993516}; OrderedLocusNames=sll1031;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP LACK OF CARBONIC ANHYDRASE ACTIVITY.
RC STRAIN=PCC 6803 / Kazusa;
RX DOI=10.1139/b05-057;
RA So A.K., Espie G.S.;
RT "Cyanobacterial carbonic anhydrases.";
RL Can. J. Bot. 83:721-734(2005).
RN [3]
RP DISCUSSION OF SEQUENCE, AND ISOFORMS CCMM73 AND CCMM52.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=17675289; DOI=10.1074/jbc.m703896200;
RA Long B.M., Badger M.R., Whitney S.M., Price G.D.;
RT "Analysis of carboxysomes from Synechococcus PCC7942 reveals multiple
RT Rubisco complexes with carboxysomal proteins CcmM and CcaA.";
RL J. Biol. Chem. 282:29323-29335(2007).
RN [4]
RP FUNCTION, INTERACTION WITH CARBONIC ANHYDRASE (CCAA); CCMK1; CCMK2; CCMK4;
RP CCML; CCMM AND CCMN, SUBCELLULAR LOCATION, MULTIPLE PROTEIN FORMS, AND
RP ISOFORM M52.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=17993516; DOI=10.1128/jb.01283-07;
RA Cot S.S., So A.K., Espie G.S.;
RT "A multiprotein bicarbonate dehydration complex essential to carboxysome
RT function in cyanobacteria.";
RL J. Bacteriol. 190:936-945(2008).
RN [5]
RP INTERACTION WITH CCAA, AND MUTAGENESIS OF 177-GLN--GLN-188.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=27729545; DOI=10.1042/bcj20160773;
RA McGurn L.D., Moazami-Goudarzi M., White S.A., Suwal T., Brar B., Tang J.Q.,
RA Espie G.S., Kimber M.S.;
RT "The structure, kinetics and interactions of the beta-carboxysomal beta-
RT carbonic anhydrase, CcaA.";
RL Biochem. J. 473:4559-4572(2016).
CC -!- FUNCTION: Functions as a scaffold protein for the assembly of beta-
CC carboxysomes, initiates carboxysome assembly via its N-terminal domain
CC binding to CcaA, CcmK and CcmL. Binds HCO(3)-, suggesting it may play a
CC role in the activity or regulation of bicarbonate dehydration
CC (PubMed:17993516). Also initiates carboxysome assembly by coalescing
CC RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) via its SSU-like
CC domains. Produced as a full-length and a shorter form; both forms are
CC required for correct carboxysome assembly and growth (By similarity).
CC Despite its strong similarity to gamma-class carbonic anhydrase (CA) it
CC does not have detectable CA activity (Ref.2, PubMed:17993516).
CC {ECO:0000250|UniProtKB:Q03513, ECO:0000269|PubMed:17993516,
CC ECO:0000269|Ref.2}.
CC -!- FUNCTION: Beta-carboxysome assembly initiates when soluble RuBisCO is
CC condensed into a liquid matrix in a pre-carboxysome by the RbcS-like
CC domains of probably both forms of CcmM. CcmN interacts with the N-
CC terminus of full length CcmM, and then recruits the shell proteins
CC (CcmK) via CcmN's encapsulation peptide. CcmM73 also interacts with
CC CcmK proteins and CcmL directly. Shell formation requires CcmK proteins
CC and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully
CC encapsulated carboxysomes are formed, they migrate within the cell
CC probably via interactions with the cytoskeleton.
CC {ECO:0000250|UniProtKB:Q03513, ECO:0000269|PubMed:17993516,
CC ECO:0000269|PubMed:27729545}.
CC -!- SUBUNIT: Probably forms homotrimers (Probable). Full length CcmM
CC interacts with CcaA, CcmK1, CcmK2, CcmK4, CcmL, CcmN and itself, while
CC the N-terminus of CcmM (first 249 residues) only interacts with CcaA,
CC CcmM and CcmN. A probable CcmM-CcaA-CcmN complex as well as a CcaA-
CC RuBisCO-CcmM complex can also be isolated (PubMed:17993516). Interacts
CC with full-length CcaA and the first 220 residues of CcaA; surface
CC residues Gln-177 to Gln-188 are responsible in part for binding
CC (PubMed:27729545). {ECO:0000269|PubMed:17993516,
CC ECO:0000269|PubMed:27729545, ECO:0000305|PubMed:17993516}.
CC -!- INTERACTION:
CC P72758; Q54735: ccaA; NbExp=6; IntAct=EBI-862848, EBI-1622341;
CC P72758; P72757: ccmN; NbExp=3; IntAct=EBI-862848, EBI-1609426;
CC P72758; P52231: trxA; NbExp=2; IntAct=EBI-862848, EBI-862916;
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000269|PubMed:17993516}.
CC Note=This cyanobacterium makes beta-type carboxysomes. Full length
CC protein associates with the shell portion of carboxysomes, CcmM52
CC associates with both the soluble and shell portion of carboxysomes.
CC {ECO:0000269|PubMed:17993516}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=CcmM73 {ECO:0000305|PubMed:17993516};
CC IsoId=P72758-1; Sequence=Displayed;
CC Name=CcmM52 {ECO:0000305|PubMed:17675289, ECO:0000305|PubMed:17993516};
CC IsoId=P72758-2; Sequence=VSP_060774;
CC -!- DOMAIN: The N-terminus has a gamma-class carbonic anhydrase-like domain
CC (CA), while the C-terminus has 4 repeats that are similar to the small
CC subunit of RuBisCO (rbcS), called SSUL. The SSUL are connected by
CC flexible linkers. The N-terminal domain forms a scaffold on which CA
CC and other carboxysomal proteins assemble, while the C-terminus binds
CC RuBisCO. {ECO:0000269|PubMed:17993516}.
CC -!- PTM: Multiple forms of the protein of 73 (full length), 62, 52 (the
CC most predominant form) and 36 kDa are seen even in the presence of
CC protease inhibitors. CcmM52 interacts with CcaA.
CC {ECO:0000269|PubMed:17993516}.
CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family.
CC {ECO:0000305|PubMed:17993516}.
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DR EMBL; BA000022; BAA16773.1; -; Genomic_DNA.
DR PIR; S74621; S74621.
DR AlphaFoldDB; P72758; -.
DR SMR; P72758; -.
DR IntAct; P72758; 14.
DR STRING; 1148.1651846; -.
DR PaxDb; P72758; -.
DR EnsemblBacteria; BAA16773; BAA16773; BAA16773.
DR KEGG; syn:sll1031; -.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG4451; Bacteria.
DR InParanoid; P72758; -.
DR OMA; RFKTKSW; -.
DR BRENDA; 4.2.1.1; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031470; C:carboxysome; IDA:UniProtKB.
DR GO; GO:0043886; F:structural constituent of carboxysome; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.190.10; -; 4.
DR InterPro; IPR017156; CcmM.
DR InterPro; IPR000894; RuBisCO_ssu_dom.
DR InterPro; IPR036385; RuBisCO_ssu_sf.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR Pfam; PF00101; RuBisCO_small; 4.
DR PIRSF; PIRSF037250; CcmM; 1.
DR SMART; SM00961; RuBisCO_small; 4.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF55239; SSF55239; 4.
PE 1: Evidence at protein level;
KW Alternative initiation; Bacterial microcompartment;
KW Carbon dioxide fixation; Carboxysome; Photosynthesis; Reference proteome;
KW Repeat.
FT CHAIN 1..687
FT /note="Carboxysome assembly protein CcmM"
FT /id="PRO_0000451242"
FT REGION 242..327
FT /note="RbcS-like repeat 1, SSUL1"
FT /evidence="ECO:0000305|PubMed:17993516"
FT REGION 328..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..445
FT /note="RbcS-like repeat 2, SSUL2"
FT /evidence="ECO:0000305|PubMed:17993516"
FT REGION 442..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..562
FT /note="RbcS-like repeat 3, SSUL3"
FT /evidence="ECO:0000305|PubMed:17993516"
FT REGION 565..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..687
FT /note="RbcS-like repeat 4, SSUL4"
FT /evidence="ECO:0000305|PubMed:17993516"
FT COMPBIAS 332..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..240
FT /note="Missing (in isoform CcmM52)"
FT /evidence="ECO:0000305|PubMed:17675289"
FT /id="VSP_060774"
FT MUTAGEN 177..188
FT /note="QQHQADSLPDVQ->AQAQADSLPAVA: Decreases affinity for
FT CcaA."
FT /evidence="ECO:0000269|PubMed:27729545"
SQ SEQUENCE 687 AA; 73121 MW; 2CD79B6058DCCECF CRC64;
MLAKSLGWLL AVSRRNYCMG SRTALASRPW SKHLADPQID PTAYVHSFAN VVGDVRIQPG
VSVAPGSSIR ADEGTPFWIG GNVLIQHGVV IHGLETGRVL GDDDQEYSVW IGPGTCVAHL
ALVHGPVYLG ANCFIGFRST VLNARVGDGA VVMMHSLVQD VEIPPNKLVP SGAMITQQHQ
ADSLPDVQAG DRHFVQQIAA MHGQSASPTQ GTDPTVCVLP ESLPAVTPVT ETPYINSIDN
MSINSDITNQ IRSLLAQGYG IGAEHANERR FKTKSWQSCG TADGFRPDQV IATVEGWLQE
FAGEYVRLIG IDQGAKRRVV EVIIQRPGDV PGSPSRGTTT TKALSSGGSG RSAVAHQTGN
LAGDSANQLR ALLHQGYKIG LEYASARRFK TGSWLTGGTI GSHREGEALQ ELNRFLADHT
NEYVRIIGID PAGKRRVAEI VVHRPNGNGN GKPSSSSSSV GYKSAPVSSA GGSSAGGLTP
EVIATVRGLL ANGHSIGTEH TDKRRFKAKS WDTCPTIDGG REAEVLAKLE ACLADHAGEY
VRIIGIDRVG KRRVLEQIIQ RPGDNVVAGR SPSSSSASTS SSASSNGFGS GNGGGYSNSA
VRLDNSVVTQ VRSLLAQGYK IGTEHTDKRR FKAKSWQSCA PITSTHESEV LRALEGCLAD
HNGEYVRLLG IDPTAKRRVL ETIIQRP
