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Database: UniProt
Entry: Q4C9T3_CROWT
LinkDB: Q4C9T3_CROWT
Original site: Q4C9T3_CROWT 
ID   Q4C9T3_CROWT            Unreviewed;       143 AA.
AC   Q4C9T3;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=ATP synthase subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
DE   AltName: Full=ATP synthase F(0) sector subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
DE   AltName: Full=ATPase subunit II {ECO:0000256|HAMAP-Rule:MF_01399};
DE   AltName: Full=F-type ATPase subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
DE            Short=F-ATPase subunit b' {ECO:0000256|HAMAP-Rule:MF_01399};
GN   Name=atpF2 {ECO:0000256|HAMAP-Rule:MF_01399};
GN   Synonyms=atpG {ECO:0000256|HAMAP-Rule:MF_01399};
GN   ORFNames=CwatDRAFT_6286 {ECO:0000313|EMBL:EAM53203.1};
OS   Crocosphaera watsonii WH 8501.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=165597 {ECO:0000313|EMBL:EAM53203.1, ECO:0000313|Proteomes:UP000003922};
RN   [1] {ECO:0000313|EMBL:EAM53203.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM53203.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   DOE Joint Genome Institute;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EAM53203.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM53203.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-ORNL);
RA   Larimer F., Land M.;
RT   "Annotation of the draft genome assembly of Crocosphaera watsonii WH
RT   8501.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAM53203.1, ECO:0000313|Proteomes:UP000003922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 8501 {ECO:0000313|EMBL:EAM53203.1,
RC   ECO:0000313|Proteomes:UP000003922};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P.;
RT   "Sequencing of the draft genome and assembly of Crocosphaera watsonii WH
RT   8501.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC       peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged
CC       and duplicated form of b found in plants and photosynthetic bacteria.
CC       {ECO:0000256|HAMAP-Rule:MF_01399}.
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation.
CC       {ECO:0000256|ARBA:ARBA00025198, ECO:0000256|HAMAP-Rule:MF_01399}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta, b and b'
CC       chains. {ECO:0000256|HAMAP-Rule:MF_01399}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01399}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01399}. Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the ATPase B chain family.
CC       {ECO:0000256|ARBA:ARBA00005513, ECO:0000256|HAMAP-Rule:MF_01399,
CC       ECO:0000256|RuleBase:RU003848}.
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:EAM53203.1}.
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DR   EMBL; AADV02000001; EAM53203.1; -; Genomic_DNA.
DR   RefSeq; WP_007303505.1; NZ_AADV02000001.1.
DR   AlphaFoldDB; Q4C9T3; -.
DR   KEGG; cwa:CwatDRAFT_6286; -.
DR   Proteomes; UP000003922; Unassembled WGS sequence.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   CDD; cd06503; ATP-synt_Fo_b; 1.
DR   Gene3D; 1.20.5.620; F1F0 ATP synthase subunit B, membrane domain; 1.
DR   HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR   HAMAP; MF_01399; ATP_synth_bprime; 1.
DR   InterPro; IPR034679; ATP_synth_b.
DR   InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR   InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR   PANTHER; PTHR33445:SF2; ATP SYNTHASE SUBUNIT B; 1.
DR   PANTHER; PTHR33445; ATP SYNTHASE SUBUNIT B', CHLOROPLASTIC; 1.
DR   Pfam; PF00430; ATP-synt_B; 1.
DR   SUPFAM; SSF81573; F1F0 ATP synthase subunit B, membrane domain; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01399};
KW   CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|HAMAP-Rule:MF_01399};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01399};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01399};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01399};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003922};
KW   Thylakoid {ECO:0000256|HAMAP-Rule:MF_01399};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01399};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01399};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01399}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01399"
FT   COILED          45..131
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   143 AA;  16067 MW;  95F7E26F5DE14399 CRC64;
     MFDFDATLPL MALQFILLAI ILNAIFYKPL NKALDERADY IRQKQSGGQK ELAEAKELAA
     QYEQQLAEAR KQSQEIVAQA QSEAKQLASE AVAEAQREAI AKKEAAAQEI EQQRQEALKT
     LEQQVDTLSR QILEKLLGPE LVK
//
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