CCMN_SYNY3
ID CCMN_SYNY3 Reviewed; 241 AA.
AC P72757;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Carboxysome assembly protein CcmN {ECO:0000305};
DE AltName: Full=Carbon dioxide concentrating mechanism protein CcmN;
GN Name=ccmN {ECO:0000303|PubMed:17993516}; OrderedLocusNames=sll1032;
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 INTERACTION WITH CCMM.
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).
CC -!- FUNCTION: Required for carboxysome formation; the N-terminus interacts
CC with CcmM which itself binds RuBisCO (ribulose bisphosphate
CC carboxylase, rbcL-rbcS) (PubMed:17993516). May also contact shell
CC protein CcmK to help assemble the carboxysome (By similarity).
CC {ECO:0000250|UniProtKB:P46204, ECO:0000269|PubMed:17993516}.
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 CcmK major shell
CC protein via CcmN's encapsulation peptide. Shell formation requires CcmK
CC proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once
CC fully encapsulated carboxysomes are formed, they migrate within the
CC cell probably via interactions with the cytoskeleton.
CC {ECO:0000250|UniProtKB:P46204}.
CC -!- SUBUNIT: Interacts with full-length and the N-terminal 249 residues of
CC CcmM; a probable CcmM-CcaA-CcmN complex can also be isolated
CC (PubMed:17993516). Interacts with CcmK (By similarity).
CC {ECO:0000250|UniProtKB:P46204, ECO:0000269|PubMed:17993516}.
CC -!- INTERACTION:
CC P72757; P72758: ccmM; NbExp=3; IntAct=EBI-1609426, EBI-862848;
CC -!- SUBCELLULAR LOCATION: Carboxysome {ECO:0000305|PubMed:17993516}.
CC Note=This cyanobacterium makes beta-type carboxysomes.
CC {ECO:0000305|PubMed:17993516}.
CC -!- SIMILARITY: Belongs to the CcmN family. {ECO:0000305}.
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DR EMBL; BA000022; BAA16772.1; -; Genomic_DNA.
DR PIR; S74620; S74620.
DR AlphaFoldDB; P72757; -.
DR SMR; P72757; -.
DR IntAct; P72757; 10.
DR STRING; 1148.1651845; -.
DR PaxDb; P72757; -.
DR EnsemblBacteria; BAA16772; BAA16772; BAA16772.
DR KEGG; syn:sll1032; -.
DR eggNOG; COG0663; Bacteria.
DR InParanoid; P72757; -.
DR OMA; TLFPHRQ; -.
DR PhylomeDB; P72757; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0031470; C:carboxysome; IEA:UniProtKB-SubCell.
DR GO; GO:0043886; F:structural constituent of carboxysome; IEA:UniProt.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW Bacterial microcompartment; Carbon dioxide fixation; Carboxysome;
KW Photosynthesis; Reference proteome.
FT CHAIN 1..241
FT /note="Carboxysome assembly protein CcmN"
FT /id="PRO_0000451245"
FT REGION 123..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..241
FT /note="Encapsulation peptide"
FT /evidence="ECO:0000250|UniProtKB:P46204"
FT COMPBIAS 123..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 25057 MW; 2555A88B4EB8B9D4 CRC64;
MQLPPVHSVS LSEYFVSGNV IIHETAVIAP GVILEAAPDC QITIEAGVCI GLGSVISAHA
GDVKIQEQTA IAPGCLVIGP VTIGATACLG SRSTVFQQDI DAQVLIPPGS LLMNRVADVQ
TVGASSPTTD SVTEKKSPST ANPIAPIPSP WDNEPPAKGT DSPSDQAKES IARQSRPSTA
EAAEQISSNR SPGESTPTAP TVVTTAPLVS EEVQEKPPVV GQVYINQLLL TLFPERRYFS
S